FOLDING AND DYNAMICS OF MELITTIN IN REVERSED MICELLES

被引：8

作者：

BISMUTO, E ^{[1
]}

SIRANGELO, I ^{[1
]}

IRACE, G ^{[1
]}

机构：

[1] UNIV NAPLES,DIPARTIMENTO BIOCHIM & BIOFIS,VIA COSTANTINOPOLI 16,I-80138 NAPLES,ITALY

来源：

BIOCHIMICA ET BIOPHYSICA ACTA | 1993年 / 1146卷 / 02期

关键词：

REVERSED MICELLE; MEMBRANE MELITTIN INTERACTION; MELITTIN FOLDING; FREQUENCY DOMAIN FLUOROMETRY; FLUOROMETRY; LIFETIME DISTRIBUTION;

D O I：

10.1016/0005-2736(93)90358-7

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The main structural characteristics and the dynamic properties of melittin bound to the internal surface of reversed micelles, formed by sodium bis(2-ethyl-1-exyl)sulfosuccinate (AOT) in isooctane, were investigated by several spectroscopic techniques. Melittin has been found associated to reversed AOT micelles in a single state, thus indicating that this system behaves differently with respect to phospholipid vesicles where at least two forms of lipid associated melittin are observed. The dynamic properties of melittin in reversed AOT micelles at different water contents were examined by frequency domain fluorometry. The whole emission decay was analyzed in terms of lifetime distribution having a Lorentzian shape. The results indicated that the binding of melittin to inverted micelles determines an increase of emission heterogeneity compared to that observed for the fully extended helical monomer. This was explained in terms of a larger variety of microenvironmental conditions that the tryptophan residue experiences during its excited state. However, the conformation freedom of the peptide can be modulated by varying the micellar size.

引用

页码：213 / 218

页数：6

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