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

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

doi:10.1039/c4sm01793e

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

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

Clinical Chemistry, Malmö

Research output: Contribution to journal › Article › peer-review

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.

Original language	English
Pages (from-to)	414-421
Journal	Soft Matter
Volume	11
Issue number	2
DOIs	https://doi.org/10.1039/c4sm01793e
Publication status	Published - 2015

Subject classification (UKÄ)

Medicinal Chemistry

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10.1039/c4sm01793e

http://www.ncbi.nlm.nih.gov/pubmed/25408475?dopt=Abstract

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title = "A peptide from human semenogelin I self-assembles into a pH-responsive hydrogel.",

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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AU - Frohm, Birgitta

AU - DeNizio, J E

AU - Lee, D S M

AU - Gentile, L

AU - Olsson, U

AU - Malm, Johan

AU - Akerfeldt, K S

AU - Linse, S

PY - 2015

Y1 - 2015

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AB - 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.

U2 - 10.1039/c4sm01793e

DO - 10.1039/c4sm01793e

M3 - Article

C2 - 25408475

SN - 1744-6848

VL - 11

SP - 414

EP - 421

JO - Soft Matter

JF - Soft Matter

IS - 2

ER -

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

Abstract

Subject classification (UKÄ)

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