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

Frohm, Birgitta; DeNizio, J E; Lee, D S M; Gentile, L; Olsson, U; Malm, Johan LU ; Akerfeldt, K S and Linse, S (2015) In Soft Matter 11(2). p.414-421
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... (More)
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. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Soft Matter
volume
11
issue
2
pages
414 - 421
publisher
Royal Society of Chemistry
external identifiers
  • pmid:25408475
  • wos:000346060400021
  • scopus:84916895131
ISSN
1744-6848
DOI
10.1039/c4sm01793e
language
English
LU publication?
yes
id
b459a1f5-6216-4ed6-bea8-f8a19fd203de (old id 4816411)
alternative location
http://www.ncbi.nlm.nih.gov/pubmed/25408475?dopt=Abstract
date added to LUP
2014-12-03 14:37:38
date last changed
2017-08-20 03:06:20
@article{b459a1f5-6216-4ed6-bea8-f8a19fd203de,
  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.},
  author       = {Frohm, Birgitta and DeNizio, J E and Lee, D S M and Gentile, L and Olsson, U and Malm, Johan and Akerfeldt, K S and Linse, S},
  issn         = {1744-6848},
  language     = {eng},
  number       = {2},
  pages        = {414--421},
  publisher    = {Royal Society of Chemistry},
  series       = {Soft Matter},
  title        = {A peptide from human semenogelin I self-assembles into a pH-responsive hydrogel.},
  url          = {http://dx.doi.org/10.1039/c4sm01793e},
  volume       = {11},
  year         = {2015},
}