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Colloids Surf B Biointerfaces. 2007 Oct 15;60(1):55-61. Epub 2007 Jun 2.

Fibril formation of lysozyme upon interaction with sodium dodecyl sulfate at pH 9.2.

Author information

1
Institute of Biochemistry and Biophysics, University of Tehran, Tehran, Iran. moosavi@ibb.ut.ac.ir

Abstract

Fibril formation seems to be a general property of all proteins. Its occurrence in hen or human lysozyme depends on certain conditions, namely acidic pHs or the presence of some additives. This paper studies the interaction of lysozyme with sodium dodecyl sulfate (SDS) at pH 9.2, using UV-visible spectrophotometry, circular dichroism (CD) spectropolarimetry, electron microscopy (EM) and chemometry. Based on observations such as the strange increase in absorbance at 650nm (pH 9.2) and the presence of intermediates, it is assumed that lysozyme fibrils have been formed at pH 9.2 in the presence of SDS as an anionic surfactant. Thioflavin T emission fluorescence and an EM image confirmed this assumption. beta-cyclodextrin was then used as a turbidity inhibitor to establish its effect on the distribution of intermediates that participate in fibril formation.

PMID:
17616361
DOI:
10.1016/j.colsurfb.2007.05.018
[Indexed for MEDLINE]

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