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

Frohm, B; DeNizio, J E; Lee, D S M; Gentile, L; Olsson, U; Malm, J; Akerfeldt, K S; Linse, S · Soft Matter · 2015

basic_science · Level V

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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.

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