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Soft Matter. 2015 Jan 14;11(2):414-21. doi: 10.1039/c4sm01793e.

A peptide from human semenogelin I self-assembles into a pH-responsive hydrogel.

Author information

1
Biochemistry and Structural Biology, Lund University, P O Box 124, SE-221 00 Lund, Sweden. sara.linse@biochemistry.lu.se.

Abstract

The peptide GSFSIQYTYHV derived from human semenogelin I forms a transparent hydrogel through spontaneous self-assembly in water at neutral pH. Linear rheology measurements demonstrate that the gel shows a dominating elastic response over a large frequency interval. CD, fluorescence and FTIR spectroscopy and cryo-TEM studies imply long fibrillar aggregates of extended β-sheet. Dynamic light scattering data indicate that the fibril lengths are of the order of micrometers. Time-dependent thioflavin T fluorescence shows that fibril formation by GSFSIQYTYHV is a nucleated reaction. The peptide may serve as basis for development of smart biomaterials of low immunogenicity suitable for biomedical applications, including drug delivery and wound healing.

PMID:
25408475
DOI:
10.1039/c4sm01793e
[Indexed for MEDLINE]

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