Fluorescent alamethicin fragments a study of membrane activity and aqueous phase aggregation

Balaram, P. ; Mathewa, M. K. ; Nagaraj, R. (1981) Fluorescent alamethicin fragments a study of membrane activity and aqueous phase aggregation Biochimica et Biophysica Acta: Biomembranes, 649 (2). pp. 336-342. ISSN 0005-2736

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Official URL: http://linkinghub.elsevier.com/retrieve/pii/000527...

Related URL: http://dx.doi.org/10.1016/0005-2736(81)90423-5

Abstract

The linear polypeptide antibiotic alamethicin is known to form channels in artificial lipid membranes. Synthetic 13- and 17-residue alamethicin fragments, labelled with a fluorescent dansyl group at the N-terminus, have been shown to translocate divalent cations across phospholipid membranes and to uncouple oxidative phosphorylation in rat liver mitochondria, in a manner analogous to the parent peptides. From studies of the aqueous phase aggregation behavior of the peptides, as well as their interaction with rat liver mitochondria, it is concluded that the interaction of the peptides with membranes is a complex process, probably involving both aqueous and membrane phase aggregation.

Item Type:Article
Source:Copyright of this article belongs to Elsevier Science.
Keywords:Alamethicin Fragment; Membrane-active Peptide; Phase Aggregation Behavior; Fluorescence
ID Code:4949
Deposited On:18 Oct 2010 06:11
Last Modified:16 May 2016 15:31

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