Episode 13 of the Modern Chemistry podcast features Dr. Silvia Marchesan, Associate Professor the University of Trieste, Italy (Università degli Studi di Trieste) and head of the SuperStructures Lab. Prior to her current position, Silvia has worked in the UK and Australia, using a range of biology and chemistry techniques. Her current research focus includes the self-assembling properties of superstructures, and how to design the necessary building blocks that create those structures.
You will hear the following terms used during the interview. I've included some descriptions here.
We discussed the drawing of Alice going through the looking glass during our discussion, you can see it at https://www.sciencephoto.com/media/995913/view/through-the-looking-glass-alice-pushes-through-the-mirror.
Silvia also mentions an article in the journal ACS Nano, you can find that at: https://pubs.acs.org/doi/10.1021/acsnano.0c09386#
Silvia is contactable on social media, you can find her on
LinkedIn https://www.linkedin.com/in/silvia-marchesan-2590712/
On Twitter, search @MarchesanLab
The group website is www.marchesanlab.com
Our theme music is "Wholesome" by Kevin MacLeod (https://incompetech.com)
Music from https://filmmusic.io
License: CC BY (http://creativecommons.org/licenses/by/4.0/)
Connect with me (Paul) at https://www.linkedin.com/in/paulorange/
H.E.L. group can be found at www.helgroup.com online,
on LinkedIn at https://www.linkedin.com/company/hel-group/
on Twitter we're @hel_group, https://twitter.com/hel_group
or search for us on Facebook
Paul Orange (00:00):
Hello, and welcome to the Modern Chemistry podcast, with your host, Paul Orange. Hello, everyone, and welcome to episode number 13 of the Modern Chemistry podcast. I'm your host for today's show, Paul Orange. Today on the show I talk to Silvia Marchesan, and Silvia is an Associate Professor at the University of Trieste, in Italy. She runs the Superstructures Lab there. As you'll hear during our discussion, a big focus of the work of the lab is looking at self-assembling super structures or super molecules. These super structures have a huge range of applications, everything, potentially, from chemical processes where they can be used as catalysts, through to medicinal uses where they can actually be used as therapeutic agents with some very interesting properties.
Paul Orange (00:57):
In particular, you'll hear us talk about the design of the subunits and the building blocks of these super molecules, and how that affects the ultimate function and can confer specific properties on the final molecule. If you're interested in further reading, there will be links in the show notes, but I would recommend checking out the group's website, which is marchesanlab.com. Again, I will put a link to that in the show notes. I'm going to hand over to Silvia in a moment, but a couple of quick points before I do.
Paul Orange (01:28):
Firstly, I will be back at the end with some exciting news about the next podcast, which I think is a really nice complement and follow on from the discussion that we have today. Secondly, just to say that today's interview starts slightly unusually, Sylvia and I were having a pre-interview chat, and we got onto the topic of using social media in science communication. I just thought that was really useful to leave in because science communication is an ever increasingly important topic, especially with all the different channels we have available to us. It's a couple of minutes or so, and I know I don't sound particularly warmed up during this first couple of minutes, I get there. Please bear with me during those first couple of minutes. But with that, I'm going to hand you straight over to Silvia and I'm going to be back at the end.
Silvia Marchesan (02:17):
I've listened to your podcast-
Paul Orange (02:19):
Thank you. I appreciate that.
Silvia Marchesan (02:21):
... with Vittorio, I really enjoyed it. I also listened to part of it with Nessa.
Paul Orange (02:30):
You know Nessa as well?
Silvia Marchesan (02:32):
I mean, only through Twitter.
Paul Orange (02:36):
Everybody does.
Silvia Marchesan (02:37):
I think these days social media is really important. Also scientists, we need to engage with the public, and I think it's also our duty to try to engage and use social media tools, because that's the thing now.
Paul Orange (02:58):
Exactly.
Silvia Marchesan (02:58):
It's not always easy. Because I think it can be easy to get things wrong, so one has to be a little bit careful.
Paul Orange (03:05):
Sure.
Silvia Marchesan (03:05):
You try, you learn.
Paul Orange (03:08):
I have to admit something. I mean, I was a scientist many years ago, and I think one of the reasons that I moved away from doing practical sciences, I was never very good at the background reading, so reading publications. It's not my cup of tea at all. I lost myself in reading, I got to about an hour and a half of looking through the work you're doing and it was a rabbit hole, it's fascinating. I'm really interested to dig into this. I was really-
Silvia Marchesan (03:51):
I realized that maybe when I told you about the things we do, I tackled it more from, let's say a storyteller point of view, because usually that works very effectively, especially with the general public and with schools. They like stories, it helps them to follow the science. But perhaps you wanted something more practical, more pragmatic about what we do, and why we do it, and what can we do with these things and so on.
Silvia Marchesan (04:21):
But I'll just tell you. Basically, our lab, it's called Superstructures Lab, because we're really interested in assembling things together starting from molecules and sometimes getting aid also with nanomaterials. Other times, we form the nanomaterials with the molecules that self-organize. When the structures become way, way bigger than the building blocks that compose them, then you can call them super structures. Like Lego, is so fascinating, you can use Lego blocks and make all sorts of things. Now there's even exhibitions, art exhibitions, that go around the big museums in the world to show you how you can really make big spaceships or monuments out of Lego blocks and so on.
Silvia Marchesan (05:10):
We would really love to be able to combine different components and really build functional architectures, and perhaps architectures can move and they can adopt into different things over time as required. But I would say we're still trying to understand, really, how these molecules behave and how we can control their behavior. We're not quite where we'd like to be, I think there's still a long way ahead. We're also interested in keeping an eye on sustainability. The materials that we develop, we need a solvent because molecules need to move first to have a solvent where they can move to organize.
Silvia Marchesan (05:51):
We work especially with water as a solvent. Sometimes we use acetonide trial as a green solvent. But we try to stay away from all the other options that are less environmentally friendly, let's say. We focus on the use of biomolecules, short peptides, things that will not persist in the environment, and also building blocks that are extremely simple to make. I was listening to Vittorio's podcast, and I realized we have more things in common than I thought, because some of the keywords he was using, such as simplicity, cast, and to do something that can be really taken up also by lower income countries and so on. Those are also our priorities.
Silvia Marchesan (06:40):
Of course, we're not perfect. Sometimes we have to compromise a little bit, make compromises. For example, we make the peptides by solid-phase peptide synthesis, which is not really the most environmentally friendly choice. However, it's very efficient, and especially when we have junior scientists, it's the most efficient way for them to get the building blocks to work with them. We're also developing new ways to make this materials, for example, using enzymes or even using microwave reactors with reactions using water solvent. It's tricky. We'll need further research in those areas. But we are aware that our process is not perfect from start to end. We're aware of the places where we can improve in terms of sustainability, and we're working on it.
Silvia Marchesan (07:38):
What do we do with these materials? Well, really, we focus on how these short peptides, peptides made of two amino acids, three amino acids, really simple molecules, how they can come together and form different nano structures. We have recently published an article on ACS Nano, where we have shown that a specific sequence of a tripeptide was affecting in inhibiting the fibrillization of amyloid-β peptide, which is associated with Alzheimer's disease. This is because the sequence has two amino acids that, if you like, act as bait, they bind to a motif in the β peptide associated with Alzheimer's disease.
Silvia Marchesan (08:30):
Then there is another amino acid which acts as a breaker, it doesn't favor the formation of these fibrils. The combination of these two things together, basically makes this peptide self-assemble into nanoparticles. When we tested it on amyloid-β peptide, we could see inhibition of the fibrillization. Of course, these experiments are just in vitro, so there's still a long way to go. But it's a good start, it's a promising start.
Silvia Marchesan (09:03):
We're also trying to mimic enzymes. We have identified short peptides that when they are in solution, they are not active as catalysts. But when they self-assemble into these big structures, then they can become catalytically active. These self-assembly works, it's hydrophobically driven. These hydrophobic molecules don't like water too much, and they like to come together. But then you have to design them appropriately so that they don't just precipitate out of the solution, but actually they can cooperate with each other and engage and form these functional structures. When that happens, you can have the creation of hydrophobic pockets like you have in an enzyme. If you have peptides, you can have all sorts of functional groups to catalyze reactions. You can start to think about the catalytic triads and catalytic functional groups that you have in enzymes, or you can also think of synthetic groups that you could add. For example, but I will not go too much in detail because it's still all in the making.
Paul Orange (10:12):
Okay. Fair enough.
Silvia Marchesan (10:13):
Let's say you can have functional groups that are not normally present in nature and you can encode new catalytical functions in these structures. It gets interesting because if then the catalytic activity is present only in the superstructure, because it's held together by weak bonds, low energy noncovalent bonds, then you can easily disassemble it and reassemble it once you learn how you can switch that. You can use a variety of switches, changes in pH, changes in temperature, chemical switches, light, all sorts of things.
Silvia Marchesan (10:53):
Then you can switch the system on and off, so you can assemble it and disassemble it. And so it assembles, it exerts a function, it catalyzes a reaction, for instance, or it inhibits the biological process or something else of interest. Then you don't want to use it anymore and then you disassemble it. I think the whole concept is interesting also, from the sustainability point of view, because just like when you go in a room, you switch on the light only when you need it, right, and then you switch it off when you get out of the room.
Silvia Marchesan (11:25):
Similarly, I think it's interesting if you develop systems that do not keep an activity on all the time, for example, with traditional catalysts or traditional drugs, but actually, you can switch it on only when you need it. Another area where we are working, but it will depend also on the funding that we attract, that'll we manage to secure. We're very much interested in antimicrobial systems. We found that some of these peptides can self-organize and form channels, quite big channels, water channels, so water can pass through. Then they have a hydrophobic exterior. It would be really interesting if we could insert these channels in membranes, for example in bacteria membranes. We noted that some of these systems are antimicrobial, so bacteria don't like them, but only when they are in the assembled state.
Silvia Marchesan (12:26):
These days, one of the many issues we have is that there's lots of antimicrobial resistance, so we don't have many new antibiotics, and many of the antibiotics that we have are less effective than they used to be because bugs have learned how to bypass their activity and have become resistant. This problem is not going away, because we also have the problem of pollution of land and waters with drugs, expired drugs, unused drugs and so on, that keep a low activity in the environment, and then bugs become smarter and antibiotics less effective. It's really an emergency. Not many pharma companies are investing in antibiotics, because it's quite a difficult sector that requires a lot of investment.
Silvia Marchesan (13:24):
We think it would be really innovative if we could have these very simple building blocks that on their own are not antimicrobial, and then you can switch them on, have antimicrobial activity as long as you need it, and then when you don't need it anymore, you switch them off. We're also working on irreversible switches. How we can convert one of these self-assembling systems into something that does not assemble anymore, so then even if you release it in the environment, it will not regain antimicrobial activity. These are the kind of areas where we are working.
Paul Orange (14:01):
We have a little bit of a tie in, obviously on the Zoom. But in that last example, basically then, you would use that molecule, it would assemble once, do a job, and then when it disassembled that would never come back together again?
Silvia Marchesan (14:15):
Exactly.
Paul Orange (14:16):
Right. Then you don't build up that low level of activity that can drive resistance in-
Silvia Marchesan (14:23):
Exactly. That's the concept.
Paul Orange (14:26):
Oh.
Silvia Marchesan (14:26):
We're working both on reversible and irreversible switches, because for things like catalysts, you want to reuse it, so you want reversible switches. But then if you think of the final disposal of your material, you really want to be able to switch it off irreversibly, whatever it does, be it catalysis or be it anti-microbial activity, and so on.
Paul Orange (14:46):
Right.
Silvia Marchesan (14:47):
This is the kind of things that we do. I didn't say one important aspect, and that is that one caveat of peptides is that, traditionally, they haven't been really good for drug candidates, for example, because they are easily cut off by enzymes, so they don't last in your body if you wanted to use them as drugs. However, what we do is we combine L-amino acids, which are the common amino acids, the building blocks of proteins, with their mirror image, the D-amino acids, which are much rarer, although they do occur in nature.
Silvia Marchesan (15:30):
This choice, first of all, it helps us with designing how these molecules can self-assemble and form these structures. But also, it's important because it extends the lifetime of these materials. Eventually, they will get biodegraded, but it takes a lot longer and you can fine tune the time that it takes enzyme to eat up basically this systems by choosing the design, so by choosing how many D-amino acids you place, which ones, where, but also how tight are these supramolecular structures. Because we found when they're really tight, enzymes have a harder way to get through and find the bonds that they need to hydrolyze.
Paul Orange (16:16):
Right. I guess, for anybody who's not familiar, when you talk about L&D amino acids-
Silvia Marchesan (16:22):
Yes.
Paul Orange (16:22):
... I did a little bit of research going back into my brain. Essentially, amino acids can be thought of like your hands. Right? Your left and-
Silvia Marchesan (16:31):
Yes.
Paul Orange (16:31):
... your right hand are mirror images of each other. But you can't put one on top of the other, you can't swap your left hand for your right hand, the left and right. Normally, we have this L-form, which is the majority, and like you say, the mirror image. They do occur in nature, but they're not commonly used by living organisms. Right?
Silvia Marchesan (16:51):
That's correct. This is really important. As you have a left hand and a right hand, you also have a left foot and a right foot. I think with the feet, it works better when you think of the fact that the shoes, your left shoe is not designed for your right foot. Your right foot will really have a hard time if you try to fit it into a left shoe. This is important because it's sort of the basis of biological recognition. There is a large portion of molecules, even in your body, that are chiral, they're like the hands or the feet, they look like each other but you cannot put one on top of each other. This property, the chirality, you can imagine a mirror, they're mirror image of each other, but not superimposable. This is important for molecular recognition.
Silvia Marchesan (17:48):
Molecules within your body can be recognized by other molecules and recognize each other, and this ensures that things work. This mechanism of biological recognition is also the basis of the activity of many drugs. Not all drugs, but a vast majority of drugs are chiral. This is important, so they get recognized by their target in your organism where they exert their activity. So it's important for selectivity to reduce side effects and things like that. The kind of questions we are asking is what happens when you play a little bit with this systems? In your body, you will have mainly L-amino acids that form L-peptides. Left-handed amino acids are the building blocks of left-handed peptides, that are the building blocks of left-handed proteins and enzymes. The kind of questions we ask is what happens when you insert a D-amino acid or two D-amino acids, so two mirror images inside, and you play a bit of a mirror game. A drawing that I really like, it's a pity we don't have videos in this because we are so dependent on images.
Paul Orange (19:03):
I was going to say if there's a link or something, I can put it in the show notes so that people can go and have a look.
Silvia Marchesan (19:10):
I'll do that. There is a beautiful drawing that is in London. It's one of the original drawings by John Tenniel, for the book of Alice in Wonderland, written by Lewis Carroll, at the British Library. In one of the books, Alice returns to Wonderland by stepping through the mirror, and there is this beautiful drawing where you have, on one side, Alice in the real world that tries to step in the mirror, and on the other side, Alice that stepped into Wonderland, so she's on the other side of the mirror. And there are some common elements, so for example, there is a clock and you have the real world clock, and then the Wonderland clock that looks almost the same, but it's actually animated. I like to think of it as our systems that have some building blocks that are common to those that you find in real life, occur mainly in nature, and other building blocks that are a little bit peculiar, so that would be the D-amino acids. This really gives the system a new function, just like the clock becomes animated in Wonderland. This is the kind of things that we do.
Paul Orange (20:19):
Cool. One of the things I was going to ask you about, a little bit, with the self-assembling nature of-
Silvia Marchesan (20:25):
Yes.
Paul Orange (20:26):
... the compounds that you're studying, and I think you already answered a little bit about the mechanism that causes that assembly to do with the hydrophobicity. Two questions that then sort of come to my mind, if you think of that as, let's call it a functional molecule, whether it's a drug, or an enzyme, or whatever, does the fact that you just need to make these smaller subunits and basically put them in solution make them cheaper and easier to make? Then the second question is, how easy to understand how you program these subunits that you manufacture to get them to assemble into the super structures that you're looking for.
Silvia Marchesan (21:07):
We take inspiration from nature, because nature does self-assembly all the time. Even our bodies self-assembled. It builds functional structures such as cell membranes, for instance, by putting together different elements in an ordered way. It forms different areas, there is compartmentalization where different things occur, different chemical reactions occur. This is important to build complex processes. We take inspiration from there. Yes, of course, if you try to build a large molecule or a large structure by conventional means using, let's say, organic chemistry and form covalent bonds as you would do in a polymer, depending on the level of functionality you want to put, but things can get quite costly, and the same goes for proteins, you need a lot of skills also to handle these large molecules, to characterize them, to purify them.
Silvia Marchesan (22:02):
It is a lot cheaper if you can actually have just two, three amino acids, so just make those building blocks, and let them then do the rest of the chemistry for you. That's what we're trying to do. Definitely, a big driver is sustainability, because you do fewer synthetic steps, you use fewer resources and this is also important for the cost, because then it's a lot cheaper to make these building blocks and you can make them on a large scale and we'd like to think that this is the way to really implement this systems and bring them to market, eventually. You need something that can be produced at a low cost, on a large scale and easily.
Silvia Marchesan (22:51):
Answering your second question about how do you design these things. Well, there's lots of very smart scientists in supramolecular chemistry, that take advantage of the rigidity of, let's say, aromatic structures. You can have very rigid molecules that are more traditionally used in organic chemistry. Because they're very rigid, so maybe they look a little bit more like the Lego blocks. You know the kind of angles that they have and you can, I think, more easily, think of how you can interlock them with each other to build bigger things. Peptides are quite naughty, because they're very-
Paul Orange (23:37):
Right.
Silvia Marchesan (23:37):
... flexible molecules. They don't like all this discipline in taking a specific angle and stay like that all the time, they like to move about. Basically, you have to get to know them. I've been working in this field for about 10 years. I think, now I got to know peptides a little bit. Once you know how they behave then it becomes more easy to program them. You need to have a good compromise between hydrophobic components and hydrophilic components. And you need to put that in the design so that the molecules then can come close to each other and form these structures that segregate, let's say, hydrophilic and hydrophobic components on different parts because this provides them with stability, and then can engage effectively in non-covalent interactions such as hydrogen bonds, for example, or peptide stocking. It takes a little bit of time to get to know them. But we are working hard to try to really identify design rules. Hopefully soon, we'll be able to actually put out there a large set of rules for people to design these peptides.
Paul Orange (24:58):
Wow. That's kind of amazing when you say that. Actually blows my mind, you could actually say, "Look, here's the book, right, if you follow this you can design a peptide."
Silvia Marchesan (25:10):
That's all we'd like to do. There's lots of hard work behind it.
Paul Orange (25:13):
Oh. Thank you for doing it.
Silvia Marchesan (25:17):
Well, we're not the only ones. I'm very fortunate because I have a group of young scientists that are really motivated and work hard and with passion, they really believe in what they're doing, and this is important.
Paul Orange (25:30):
You touched on something there, which I found through reading on your website and looking the background. You talk about doing simulations, and I guess, talking about rules as well lends itself to computing quite easily because you can tell a computer a very big list of very complex rules and it will understand them. How much does in silico work need to take place, or how much do you do before you then get to actually manufacturing and testing these things in wet chemistry.
Silvia Marchesan (25:59):
There's different ways to proceed. There are excellent scientists that screen in silico, and then do the chemistry, do the experiments, based on what they found from the screening. Sometimes, well, in my experience, if you want to screen really large numbers, really quickly, then you need to take some shortcuts, you need to make some compromises. When you do that, your systems may work very well on some things that are very reliable, but it may work less well on other things that are a little bit naughty. As we said, this peptides being a bit naughty, we prefer to take a different approach. When we do simulations, actually there is a collaborator of mine called [Attilio Varju 00:26:53], at the University of Calgary, he is a bio-physicist, and he does the simulations for us. He's amazing, and he doesn't take any shortcuts.
Silvia Marchesan (27:02):
He really looks atom by atom. All atoms are being simulated in explicit solvent and he runs the dynamics, I like to call it, he follows the dance of the peptides. Because they dance about and then they come together and dissociate, and then eventually they form these structures. This kind of computing gives us a great deal of detail and it's vital for what we do, because sometimes with experiments we cannot get the kind of information that simulations provide us. We also like to validate them. We take the models and, for example, we calculate theoretical spectra, that then we match with experimental spectra as a checkpoint, are the simulations truthful? This is important.
Silvia Marchesan (27:57):
We do not run simulations to screen large numbers, we do it more ad hoc to ask specific questions, as in we think this peptide is particularly interesting, it binds to amyloid-β peptide for instance, how does it behave in water? Then we really go in detail and see how it behaves and what happens when it binds to a beta, and then we validate this with experiments and so on. This is our approach now. In the future, once we get larger and larger libraries of compounds, I'd really like to go towards machine learning and try to develop systems where basically we will use in silico methods to look at the properties, let's say, for example, spectra of all these peptides that assemble, and try to identify specific signature, trying to learn new things that will help us identify even new sequences that we haven't thought about. But in order to do that, we need large numbers to start first to have really reliable systems.
Paul Orange (29:06):
Sure.
Silvia Marchesan (29:06):
I think we need to make more and more examples. Then once we reach a critical threshold of having a large enough libraries, then surely we'd love to use more in silico methods to learn more and to let the computers learn for us. So yes, I think in silico is very, very important. In the past, maybe in silico methods were not so refined as they are now. From my experience, some scientists are a little bit skeptical, perhaps, but I think modern molecular models, methods, and in silico techniques are so refined, they're so advanced, that they really are reliable and we can learn a lot from them. I think it's important to combine them with experimental techniques.
Paul Orange (29:52):
Cool. Changing direction a little bit.
Silvia Marchesan (29:55):
Yes.
Paul Orange (29:55):
Have you come across any unexpected properties of any of the super structures that have been formed? I think I read in one of your publications about one of your superstructures forms a gel and then becomes catalytically active as a gel, not when it's in solution, and that my mind kind of couldn't quite understand how does sort of a semi-solid gel have activity that-
Silvia Marchesan (30:24):
We're still trying to understand the systems, there's lots to learn. The idea behind is that if you think of proteins and the way they activate, for example the functional groups in the catalytic sites, you have a lot of interactions, and then you have a hydrophobic environment, and both aspects can alter the properties of a functional group. For example, if you have a group that tends to donate or take up a proton, then that ability will be changed dramatically by the environment of the active site of the enzyme. Similarly, the idea is that if you take certain functional groups and you insert them into these self-assembling sequences, then in the supramolecular structure you may have hydrophobic pockets, or you may have extended natural because of hydrogen bonding, for example, or other types of interactions. These can activate your functional group in a way that takes inspiration from enzymes, lets say.
Silvia Marchesan (31:31):
But it's not always straightforward to anticipate what will happen when molecules come together. And so it's not so easy to design a large variety of catalysts with this approach. We are learning as we go. Sometimes, yes, things can be unexpected. At times you can think of an enzyme and see, "Okay, in the catalytic triad there is a serine. Let's take a serine, that's an amino acid, put it in the system, it will work better." And then sometimes it doesn't, because it's just in the wrong place. That's when you need to go back to the board and think a little bit harder and use a combination of in silico and experimental techniques to try to understand why did and it didn't work? How these molecules come together in the assemblies, what can we do to change that?
Paul Orange (32:21):
I'm just aware of time.
Silvia Marchesan (32:23):
Yes.
Paul Orange (32:23):
One of the things that I like to ask the guests on the show is just a little bit about their career path and how they got here. Especially if there are younger scientists listening, just to understand the path ahead. Unlike many people I've spoken to, you've had the experience of working in many different places around the world to get to your position today. How important do you think it is to develop a career that you do go and work in different places and different labs?
Silvia Marchesan (33:00):
It's important, but I think it's important also for happiness. At least it worked in my case.
Paul Orange (33:08):
That's a very important reason.
Silvia Marchesan (33:11):
Well, in my experience, it certainly helped the fact that I traveled, but it also helped the fact that I tried to follow my instinct, my motivation, my curiosity. I tried to do the things that I wanted to do, even though it meant going to another country, travel and reinvent myself in a way. I graduated in Trieste in Italy, in this gorgeous place, as we were saying, because it's nestled between the Mediterranean Sea and the Alps, in medicinal chemistry. Then I wanted to see the world, so I moved to UK. Back then it was a little bit easier than these days. I had a brief spell at a multinational company in R&D, for summer internship, in Northern England. Then I was fortunate to get a PhD scholarship. I did my PhD at the University of Edinburgh, and that was in Scotland, and that was midway between organic chemistry and molecular biology.
Silvia Marchesan (34:18):
I started to learn also how to play with cells and recombinant DNA, and I thought that was really fascinating. Then I was actually happy to settle in Edinburgh, but my supervisor, just one year after I started the PhD, moved to London. So the whole group moved to London, and I spent two years there. London is very vibrant, I learned to be quick in London. After that I went on for a postdoc in cell biology in Finland at the University of Helsinki. I wanted to learn about the Scandinavian culture. Actually, I would say, I think in retrospectively, that that was really when I started to work with supramolecular chemistry, because I was looking at protein peptide interactions that are responsible for basically the mechanisms of cells when they stick on to something and when they move.
Silvia Marchesan (35:11):
Then after that I went to Australia, really inspiring place. I had a joint postdoc fellowship between CSIRO, which is Australia's national science agency, and Monash University in Melbourne. There it was great because, again, I had a multidisciplinary training. I was doing organic chemistry, electrospinning, got trained in the cleanroom micropatterns using XPS, maneuvering this robotic hand within the XPS instrument. It was great. Then studying how cells were responding to the materials we were making. There I was working on biomaterials for tissue regeneration.
Silvia Marchesan (35:56):
After all this traveling around the world, it was time to get closer to my family. I returned to Italy and I managed to secure a tenure track position, and then got tenure. Now I'm Associate Professor at the University of Trieste, which is right at the border, so when I need to go abroad and see new places I can easily do that.
Paul Orange (36:20):
Which, as we talked about earlier on, is something I found out when improving my geography knowledge by actually locating Trieste on the map.
Silvia Marchesan (36:27):
Yes. There's lots of diversity. I think this whole process was important, because whenever one has to relocate abroad, you are forced to think a little bit differently, you cannot rely on your contacts anymore, around we have family and friends that can help us in the case of need. It really forces you to think in new ways to troubleshoot and solve your problems on your own, so you grow a lot. I think also being exposed to different cultures, it could be different disciplines of science, or it could be different cultures in other countries, I think also that forces you to think differently. It makes you a better scientist, and I think it can also make you a better human if you learn to be more tolerant and to embrace new cultures and embrace diversity.
Paul Orange (37:19):
Well said. I agree. Silvia, again, I'm aware of time. I think we should wrap up there.
Silvia Marchesan (37:26):
Yes. You're more than welcome to visit us. Thank you for the opportunity to talk about our work and best wishes for everything.
Paul Orange (37:35):
Thank you. Your passion comes through, It's really exciting and anybody listening, please go and check out Silvia's website and publications, you will not be disappointed, I guarantee it. Silvia, thank you very much.
Silvia Marchesan (37:46):
Thank you.
Paul Orange (37:47):
Right. Well, that was amazing, wasn't it? Thank you very much for listening through to the end. I hope you all enjoyed that discussion with Silvia. I would heartily recommend you to check out her website and read a little bit more on the topic. Of course, I have to thank Silvia once again for her time, and especially for bearing with us during the frustrations we had where we needed to swap laptops before we were able to start recording. Also thank you to Vittorio Saggiomo, who was on the show last time. Vittorio suggested and connected me with Silvia. Vittorio, thanks very much for that.
Paul Orange (38:25):
Then speaking about connections, Vittorio also connected me with a guest for our next show, episode 14, Elisa Fadda. I just think this is a great compliment and continuation of the discussion that you just heard. Elisa does a lot of work in computational modeling, and has, fairly recently, published some really interesting work looking at the glycoprotein complex that is the spike protein of the Coronavirus, and how the makeup and the structure and the function of that spike protein has big influences on the infectivity of the virus itself. Rather than wait our typical two months, we're actually going to put that episode out in about two weeks time. So if you're listening to this episode on the day it goes live, wait a couple of weeks, which I think will be the 24th of June, and then you'll be able to hear that interview with Elisa, which I'm going to tell you now, it's another cracker.
Paul Orange (39:17):
I think that's everything for today. Again, thanks for listening. If you enjoy the show, please do leave us a review. If you subscribe, tell somebody else. Also, we're always on the lookout for great guests. Whether it's you or somebody you know who think would be a great guest for the show, please do drop us a line via the contact page at www.helgroup.com. But with that, stay safe, stay well, and I will speak to you in just a couple of weeks on the next episode of the Modern Chemistry podcast.
Paul Orange (39:53):
Thanks for listening to the Modern Chemistry podcast. Our theme music is provided by Kevin MacLeod under Creative Commons license. If you subscribe to this show you'll have the next episode dropped straight into your podcast feed.