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Modification of β-sheet forming peptide hydrophobic face: effect on self-assembly and gelation
DOI:
10.1021/acs.langmuir.5b03841
Authors:
Mohamed
Elsawy
(Manchester Institute of Biotechnology)
,
Andrew M.
Smith
(The University of Manchester)
,
Nigel
Hodson
(The University of Manchester)
,
Adam
Squires
(University of Reading)
,
Aline Fiona
Miller
(The University of Manchester)
,
Alberto
Saiani
(University of Manchester)
Co-authored by industrial partner:
No
Type:
Journal Paper
Journal:
Langmuir
State:
Published (Approved)
Published:
April 2016
Diamond Proposal Number(s):
12950

Abstract: Beta-sheet forming peptides have attracted significant interest for the design of hydrogels for biomedical applications. One of the main challenges is the control and understanding of the correlations between peptide molecular structure, the morphology, and topology of the fiber and network formed as well as the macroscopic properties of the hydrogel obtained. In this work, we have investigated the effect that functionalizing these peptides through their hydrophobic face has on their self-assembly and gelation. Our results show that the modification of the hydrophobic face results in a partial loss of the extended -sheet conformation of the peptide and a significant change in fiber morphology from straight to kinked. As a consequence the ability of these fibers to associate along their length and form large bundles is reduced leading. These structural changes (fiber structure and network topology) significantly affect the mechanical properties of the hydrogels (shear modulus and elasticity).
Journal Keywords: Self-assembly; peptide; hydrogel; nanofibres
Subject Areas:
Materials,
Biology and Bio-materials
Instruments:
B21-High Throughput SAXS
Added On:
29/04/2016 13:05
Documents:
acs.langmuir.5b03841.pdf
Discipline Tags:
Materials Science
Polymer Science
Life Sciences & Biotech
Technical Tags:
Small Angle X-ray Scattering (SAXS)