Optical spectroscopy to investigate the structure of regenerated Bombyx mori silk fibroin in solution.

Abstract:

:Fluorescence and circular dichroism spectroscopy were used to monitor the conformational transition of regenerated Bombyx mori silk fibroin (RSF) in aqueous solutions under different conditions. According to the analysis of fluorescence spectra using anilinonaphthalene-8-sulfonic acid magnesium salt (ANS) as an external probe, the destruction of the hydrophobic core prior to the secondary structure change suggests that this collapse may initiate the conformational transition from random coil to beta-sheet for RSF. The temperature dependence of the structural changes of RSF, detected by both fluorescence spectroscopy and circular dichroism, shows a reversible process upon heating and recooling, with the midpoint around 45 degrees C. The results also indicate that most of the tryptophan (Trp) residues contained in silk fibroin are concentrated on the surface of the unfolded protein. However, they will change their location in the highly ordered structure (e.g., becoming more homogeneous) with the conformational transition of silk fibroin. Moreover, our studies also suggest that the presence of water plays a crucial role during the structure changes of fibroin.

journal_name

Biomacromolecules

journal_title

Biomacromolecules

authors

Yang Y,Shao Z,Chen X,Zhou P

doi

10.1021/bm0343848

keywords:

subject

Has Abstract

pub_date

2004-05-01 00:00:00

pages

773-9

issue

3

eissn

1525-7797

issn

1526-4602

journal_volume

5

pub_type

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