A peptide from human semenogelin I self-assembles into a pH-responsive hydrogel.
(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)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/4816411
- author
- Frohm, Birgitta ; DeNizio, J E ; Lee, D S M ; Gentile, L ; Olsson, U ; Malm, Johan LU ; Akerfeldt, K S and Linse, S
- organization
- publishing date
- 2015
- 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
- pmid:25408475
- 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
- 2016-04-01 10:06:39
- date last changed
- 2022-03-19 17:23:00
@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}},
doi = {{10.1039/c4sm01793e}},
volume = {{11}},
year = {{2015}},
}