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Modification of β-sheet forming peptide hydrophobic face: effect on self-assembly and gelation

DOI: 10.1021/acs.langmuir.5b03841 DOI Help

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

Open Access Open Access

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


Discipline Tags:

Materials Science Polymer Science Life Sciences & Biotech

Technical Tags:

Small Angle X-ray Scattering (SAXS)