Literature DB >> 24302557

Effect of the surface chemistry of insulin fibrils on the aggregation rate.

Shuchen Hsieh1, Chiung-Wen Hsieh, Hsuan-Hung Chou, Chiung-Wen Chang, Ling-Ya Chu.   

Abstract

Structure transition cascade: Insulin fibrils undergo a secondary structural transition-from the α-rich to the β-rich form-upon progressively increasing the incubation time from 0.5 to ten hours. Atomic force microscopy measurements show that the fibril surface chemistry changes from hydrophilic to hydrophobic and the aggregation rate increases fivefold.
Copyright © 2014 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.

Entities:  

Keywords:  adhesion force; atomic force microscopy; fibrous proteins; hydrophobic effect; protein engineering

Mesh:

Substances:

Year:  2013        PMID: 24302557     DOI: 10.1002/cphc.201300838

Source DB:  PubMed          Journal:  Chemphyschem        ISSN: 1439-4235            Impact factor:   3.102


  2 in total

1.  The Hydration Shell of Monomeric and Dimeric Insulin Studied by Terahertz Time-Domain Spectroscopy.

Authors:  Pengfei Wang; Xiangchao Wang; Liyuan Liu; Hongwei Zhao; Wei Qi; Mingxia He
Journal:  Biophys J       Date:  2019-07-03       Impact factor: 4.033

2.  Spatially resolved spectroscopic differentiation of hydrophilic and hydrophobic domains on individual insulin amyloid fibrils.

Authors:  Tanja Deckert-Gaudig; Dmitry Kurouski; Martin A B Hedegaard; Pushkar Singh; Igor K Lednev; Volker Deckert
Journal:  Sci Rep       Date:  2016-09-21       Impact factor: 4.379

  2 in total

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