70
Views
2
CrossRef citations to date
0
Altmetric
Bio and food sciences

High pressure FT-IR spectroscopic study on the secondary structure changes in insulin amyloid fibril and aggregate

, , &
Pages 676-679 | Received 23 Aug 2009, Published online: 15 Dec 2009
 

Abstract

The pressure-induced changes in the secondary structure of two kinds of insulin aggregates, amyloid fibril and reduction-induced aggregate, were studied by using Fourier transform infrared (FT-IR) spectroscopy. The parallel β-sheet for the amyloid fibril is not unfolded, but dramatically distorted with increasing pressure up to 1.0 GPa. This structural rearrangement is elastic and does not cause the backbone amide protons involved in the parallel β-sheet to expose to an aqueous medium. The dissociation of the amyloid fibril into its monomer or oligomer is not likely to be promoted by application of high pressure. The antiparallel β -sheet of the reduction-induced aggregate remains distinct at 1.3 GPa. The whole construction is quite rigid in spite of the fact that the same origin (i.e. insulin) as the amyloid fibril is formed.

Log in via your institution

Log in to Taylor & Francis Online

PDF download + Online access

  • 48 hours access to article PDF & online version
  • Article PDF can be downloaded
  • Article PDF can be printed
USD 61.00 Add to cart

Issue Purchase

  • 30 days online access to complete issue
  • Article PDFs can be downloaded
  • Article PDFs can be printed
USD 1,965.00 Add to cart

* Local tax will be added as applicable

Related Research

People also read lists articles that other readers of this article have read.

Recommended articles lists articles that we recommend and is powered by our AI driven recommendation engine.

Cited by lists all citing articles based on Crossref citations.
Articles with the Crossref icon will open in a new tab.