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[Music]

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thanks Mike hi everyone my name is Tony

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I'm coming here from LC Earth Life

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Science Institute in Tokyo and they

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provided some swag outside so I think

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it's all gone but there's some Flyers

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out there so please take a look and I'm

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going to be talking about some

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collaborative work I've been doing with

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LC city college New York and with

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Harvard so one of the major questions

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that a lot of people in astrobiology

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feel specifically the like when people

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are interested in studying the origin of

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life are how did the prebiotic building

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blocks form and from the warm up talk

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earlier we see that yeah it's very

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interesting to think about how Mino

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acids nucleotides or lipids form and

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more specifically how did these building

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blocks specifically polymerize or

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assemble into something larger and

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useful so peptides of proteins nucleic

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acids or vesicles and specifically I'm

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very interested in amino acids and

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peptides and on the early Earth there

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have been many or it's been shown that

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there are many possibilities for the

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emergence of amino acids and peptides

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for example extraterrestrial objects or

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atmospheric discharge or hydrothermal

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vents they can produce amino acids and

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volcanic gases or mineral surfaces can

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help to catalyze the conjugation of

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these amino acids into peptides longer

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amino acid containing chains and some

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recent work has also suggested that it's

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possible that amino acids nucleotides

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and lipid precursors could have been

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present all together on the early Earth

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which suggests that not only should we

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study how each of these classes of

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molecules emerges and interacts within

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their own population but also how these

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different polymers interact with each

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other

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one interesting system that's been

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studied previously is the formation of

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coacervate switch our face separated

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species that form from the interaction

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of two oppositely charged polymers and

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if there's a poster earlier on

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codemaster base I think there might be

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another one tomorrow so interesting

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stuff and essentially one of these

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coacervate switch are what this one

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specifically is produced from mixing ATP

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and poly lysine which is a cationic

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peptide forms these segregated globules

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that actually segregate and concentrate

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RNA so here we see the localization of a

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fluorescently labeled RNA into specific

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globules in this system but so one of

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the things that about the system that is

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kind of iffy is the requirement for a

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reasonably long peptide chain which on

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the prebiotic earth it's you know way

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more likely for a smaller polymer to

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have existed and conjugated rather than

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a longer polymer so this begs the

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question now can we utilize smaller

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peptides to self-assemble into longer

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structures that have similar activities

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and similar uses as longer their

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original longer peptides so specifically

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I'm interested in seeing if we can use

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shorter peptides to self-assemble into

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perhaps of binding or scaffolding system

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for early nucleic acids DNA or RNA the

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small peptide self-assembly field was

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pioneered maybe fifteen years ago in Tel

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Aviv and they actually started from this

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peptide which is the beta-amyloid

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peptide and

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they took two of the amino acids from

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this peptide and were able to isolate it

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and grow these nano tubular structures

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so from just the simple molecule which

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is very hydrophobic it forms it's very

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favored to form these large

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self-assembled

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products so what I was interested in

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seeing if this could be done was if we

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had some mixture of dipeptides

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tripeptides and maybe some RNA if these

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peptides could by assemble into some

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type of fibrillar structure that RNA or

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DNA could bind to so in collaboration

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with a lab at City College in New York

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previously they developed a

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computational system to calculate the

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aggregation propensity of all 8,000 try

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peptides and so there are 20 amino acids

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that are present on today's earth that

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are created biologically there are

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others abiotic ones but we'll just stick

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with the 20 biotic amino acids and so

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from here basically they're able to

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probe all 8,000 tri peptide sequences

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and so for example you'd read the first

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sequence on the x-axis the second letter

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on the y-axis and then within each box

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you'd pick the third amino acid and each

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box is colored it goes from very light

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to very dark and so the darker the spot

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the greater propensity for that specific

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self-assembled structure from this study

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we chose six specific peptides to prou

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RNA binding character each of these

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peptides contains either two large

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hydrophobic groups or smaller aliphatic

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groups and each one also specifically

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contains a charged amino acid in the

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first position so that RNA or DNA which

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has a negatively charged backbone

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and bind to something that's positively

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charged when theoretically these fibers

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assemble so we well we took these

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structures and first of all studied the

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aggregation propensity of these

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structures alone and from these

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microscope images we can see a kind of

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variable character for example two of

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these tripeptides don't really form any

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fibrillar structure they form some

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strange spherical structure the ry f

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tripeptide forms these needle-like

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structures but specifically we found two

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tripeptides kyf and rff that assemble

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into these long fibrillar structures

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that are fairly dense and we can see

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here that some of these structures are

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actually fairly thick as well so these

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two tripeptides became reasonable

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candidates to test for binding of RNA so

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the next thing that we tested was we

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actually introduced a fluorescent

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labeled RNA into one of these assembled

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tripeptide systems and so you see on the

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right here this is a fluorescence

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microscope image and it appears that the

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fluorescently labeled RNA is assembling

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or is localizing to these assembled

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fibrillar structures which suggests that

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it is interacting with the fibers

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themselves preferentially rather than

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just staying in the solution similarly

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we also observed a slightly a similar

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behavior with the rff tripeptide upon

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pepti RNA binding it was a little less

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apparent and one of the things we

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learned about the rff peptide was that

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this these structures only formed under

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specific conditions in phosphate buffer

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which is not very compatible with

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magnesium which is used in a lot of RNA

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and ribosomal reactions so we went

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forward and characterized further the

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kyf tripeptide and we also found

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that not only does single-stranded RNA

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bind to these fibrillar structures but

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also double-stranded RNA a different

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length of single-stranded RNA as well as

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single-stranded DNA and so it can bind

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to many different types of nucleic acids

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actually might just work here yeah so

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here now is something interesting that

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came out from this study in that now

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that we know that these fluorescently

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labeled RNA are apparently binding to

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the assembled fibril structures we

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thought oh can we use this RNA molecule

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this fluorescence now to probe the

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dynamics of the fibrils themselves so

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here this image or this movie we're

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going to be showing it's a time course

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of a self-assembling tripeptide fibril

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structure with fluorescently labeled RNA

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that localizes to these structures so

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I'm just going to play this and you can

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see over time that there's some dynamic

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change going on with these fiber

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structures they appear to be growing and

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changing over time play that again

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of course this raises a bunch of

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interesting questions like why is it

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growing from one side is the nucleation

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site important what about the substrate

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that it's growing on but at the very

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least now we've developed a system where

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previously the people studying

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tripeptide fibril assembly didn't really

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consider studying really specifically

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the dynamics of the assembly process

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itself but now we have a direct binding

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reporter and we can further probe this

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system and kind of study interesting

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things about it it's pretty nice to look

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yeah and so one of the things that I'm

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interested in working on next is using a

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system that's been developed called

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dynamic peptide libraries which actually

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you're able to start with a pool of very

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diverse small peptides and over time you

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can select out those peptides that form

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vibrator or other macro structures and

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so in that case where we want to try to

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find other peptides that have other

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interesting assembled structures with

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assembled functions for example RNA DNA

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binding or even structures that are more

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heat stable or that assemble in under

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specific you know metal iron conditions

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and also different mineral surfaces

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scaffolded by different different things

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and also finally to see if the

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localization of RNA onto these fibrils

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can somehow affect evolution of RNA or

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even template its polymerization so I'd

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like to thank my collaborators at

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Harvard at City College New York and

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University of Strathclyde and at growing

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again in the Netherlands and also this

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is my home Institute LC I have some

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funding support from LC origins network

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Eon and Tokyo Tech and so I have to plug

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this now if you want to know more about

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LC please come talk to me so every year

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we have a symposium in January the this

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following January there's going to be a

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winter school which is a two-week

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hands-on course that will be really cool

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and year round there's workshops and

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they're always hiring so if you're

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interested in doing a postdoc over at LC

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there's information out there or also

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come please please come talk to me so

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thank you very much for all your time

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happy to take questions

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questions about your movie uh mostly was

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it come focal microscopy secondly how

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thick is the structure that's going and

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is it an artifact of the imaging that

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everything looks like parallel to the

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glass surface so this is a confocal

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microscope image second question I'm not

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sure but in a 3d in a tube structure the

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entire structure forms a gel-like state

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so it can it should be very large three

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dimensionally it could be and third

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um I don't know the answer to that and

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we're actually right now probing also

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like whether different substrates have

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some effect on the assembly properties

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um I have a question about from the

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paper published by your collaborator the

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Nature Chemistry paper in which they has

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the yeah this exact one so it seems like

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um tryptophan rich tripeptides have the

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highest propensity for forming the

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self-assemble structure because it's

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like the w w is like all the way down

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the in the left lower left-hand side and

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i was wondering why the try peptide that

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you studied don't have any trip to vent

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um yeah so these were a smattering of

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different candidates we would like I

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would like to test all of them but that

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wasn't possible and also from previous

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studies that they've done there are a

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lot of solubility issues with many of

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these really hydrophobic peptides so we

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also wanted to make sure that the

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peptides we were working with could

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actually be analyzed in some

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constructive way hey nice talk I had a

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question about the composition of the

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fibers themselves and how well you guys

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understand what those actually are and

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how thick they are for instance if are

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they single fibers or they double fibers

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or do an idea

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um I don't specifically know a lot about

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this but I'm sure that the people in the

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lab in the U n lab at New York there are

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some people that are certainly studying

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this and they probably have a much

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better idea than I would have a guess

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it seems so it seems like the fibers are

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consistent between the different runs

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that you used to create them for

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specific conditions generally yes

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they're very highly conditioned

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dependent for example changing the

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buffer system could lead to no growth or

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like much denser growth okay thanks um

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and sort of following on that I have

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another question about the the fibril

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formation there have been some

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suggestions in the literature that just

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phenylalanine amino acids themselves can

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make fibrils so I was wondering what

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would the rationale for picking

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tripeptides was and whether you think

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some of this might happen with with just

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single or double amino yeah um yeah it

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would be really interesting if single or

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double if like we could study more about

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these like single amino acid diet I

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peptide assemblies

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I guess specifically for this study we

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we just wanted to make sure to include a

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cationic group because we were looking

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for RNA binding but if you're looking

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for something else like formation of a

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gel state for whatever reason to prevent

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diffusion or something you might be able

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to select out a single peptide single

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amino acid or die peptide and so this

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dynamic peptide library technique that's

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been developed they've they're able to

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you're able to start with a lot of

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different components and select out

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something that you want so cool alright

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thank you very much thank you