Webbläsaren som du använder stöds inte av denna webbplats. Alla versioner av Internet Explorer stöds inte längre, av oss eller Microsoft (läs mer här: * https://www.microsoft.com/en-us/microsoft-365/windows/end-of-ie-support).

Var god och använd en modern webbläsare för att ta del av denna webbplats, som t.ex. nyaste versioner av Edge, Chrome, Firefox eller Safari osv.

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

Författare

  • Birgitta Frohm
  • J E DeNizio
  • D S M Lee
  • L Gentile
  • U Olsson
  • Johan Malm
  • K S Akerfeldt
  • S Linse

Summary, in English

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.

Publiceringsår

2015

Språk

Engelska

Sidor

414-421

Publikation/Tidskrift/Serie

Soft Matter

Volym

11

Issue

2

Dokumenttyp

Artikel i tidskrift

Förlag

Royal Society of Chemistry

Ämne

  • Medicinal Chemistry

Status

Published

Forskningsgrupp

  • Clinical Chemistry, Malmö

ISBN/ISSN/Övrigt

  • ISSN: 1744-6848