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Collagen-Inspired Helical Peptide Coassembly Forms a Rigid Hydrogel with Twisted Polyproline II Architecture

[Image: see text] Collagen, the most abundant protein in mammals, possesses notable cohesion and elasticity properties and efficiently induces tissue regeneration. The Gly-Pro-Hyp canonical tripeptide repeating unit of the collagen superhelix has been well-characterized. However, to date, the shorte...

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Autores principales: Ghosh, Moumita, Bera, Santu, Schiffmann, Sarah, Shimon, Linda J. W., Adler-Abramovich, Lihi
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Chemical Society 2020
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7450664/
https://www.ncbi.nlm.nih.gov/pubmed/32806033
http://dx.doi.org/10.1021/acsnano.0c03085
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author Ghosh, Moumita
Bera, Santu
Schiffmann, Sarah
Shimon, Linda J. W.
Adler-Abramovich, Lihi
author_facet Ghosh, Moumita
Bera, Santu
Schiffmann, Sarah
Shimon, Linda J. W.
Adler-Abramovich, Lihi
author_sort Ghosh, Moumita
collection PubMed
description [Image: see text] Collagen, the most abundant protein in mammals, possesses notable cohesion and elasticity properties and efficiently induces tissue regeneration. The Gly-Pro-Hyp canonical tripeptide repeating unit of the collagen superhelix has been well-characterized. However, to date, the shortest tripeptide repeat demonstrated to attain a helical conformation contained 3–10 peptide repeats. Here, taking a minimalistic approach, we studied a single repeating unit of collagen in its protected form, Fmoc-Gly-Pro-Hyp. The peptide formed single crystals displaying left-handed polyproline II superhelical packing, as in the native collagen single strand. The crystalline assemblies also display head-to-tail H-bond interactions and an “aromatic zipper” arrangement at the molecular interface. The coassembly of this tripeptide, with Fmoc-Phe-Phe, a well-studied dipeptide hydrogelator, produced twisted helical fibrils with a polyproline II conformation and improved hydrogel mechanical rigidity. The design of these peptides illustrates the possibility to assemble superhelical nanostructures from minimal collagen-inspired peptides with their potential use as functional motifs to introduce a polyproline II conformation into hybrid hydrogel assemblies.
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spelling pubmed-74506642020-08-31 Collagen-Inspired Helical Peptide Coassembly Forms a Rigid Hydrogel with Twisted Polyproline II Architecture Ghosh, Moumita Bera, Santu Schiffmann, Sarah Shimon, Linda J. W. Adler-Abramovich, Lihi ACS Nano [Image: see text] Collagen, the most abundant protein in mammals, possesses notable cohesion and elasticity properties and efficiently induces tissue regeneration. The Gly-Pro-Hyp canonical tripeptide repeating unit of the collagen superhelix has been well-characterized. However, to date, the shortest tripeptide repeat demonstrated to attain a helical conformation contained 3–10 peptide repeats. Here, taking a minimalistic approach, we studied a single repeating unit of collagen in its protected form, Fmoc-Gly-Pro-Hyp. The peptide formed single crystals displaying left-handed polyproline II superhelical packing, as in the native collagen single strand. The crystalline assemblies also display head-to-tail H-bond interactions and an “aromatic zipper” arrangement at the molecular interface. The coassembly of this tripeptide, with Fmoc-Phe-Phe, a well-studied dipeptide hydrogelator, produced twisted helical fibrils with a polyproline II conformation and improved hydrogel mechanical rigidity. The design of these peptides illustrates the possibility to assemble superhelical nanostructures from minimal collagen-inspired peptides with their potential use as functional motifs to introduce a polyproline II conformation into hybrid hydrogel assemblies. American Chemical Society 2020-08-05 2020-08-25 /pmc/articles/PMC7450664/ /pubmed/32806033 http://dx.doi.org/10.1021/acsnano.0c03085 Text en Copyright © 2020 American Chemical Society This is an open access article published under a Creative Commons Attribution (CC-BY) License (http://pubs.acs.org/page/policy/authorchoice_ccby_termsofuse.html) , which permits unrestricted use, distribution and reproduction in any medium, provided the author and source are cited.
spellingShingle Ghosh, Moumita
Bera, Santu
Schiffmann, Sarah
Shimon, Linda J. W.
Adler-Abramovich, Lihi
Collagen-Inspired Helical Peptide Coassembly Forms a Rigid Hydrogel with Twisted Polyproline II Architecture
title Collagen-Inspired Helical Peptide Coassembly Forms a Rigid Hydrogel with Twisted Polyproline II Architecture
title_full Collagen-Inspired Helical Peptide Coassembly Forms a Rigid Hydrogel with Twisted Polyproline II Architecture
title_fullStr Collagen-Inspired Helical Peptide Coassembly Forms a Rigid Hydrogel with Twisted Polyproline II Architecture
title_full_unstemmed Collagen-Inspired Helical Peptide Coassembly Forms a Rigid Hydrogel with Twisted Polyproline II Architecture
title_short Collagen-Inspired Helical Peptide Coassembly Forms a Rigid Hydrogel with Twisted Polyproline II Architecture
title_sort collagen-inspired helical peptide coassembly forms a rigid hydrogel with twisted polyproline ii architecture
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7450664/
https://www.ncbi.nlm.nih.gov/pubmed/32806033
http://dx.doi.org/10.1021/acsnano.0c03085
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