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

Mathew, MK and Nagaraj, R and Balaram, P (1981) Fluorescent alamethicin fragments A study of membrane activity and aqueous phase aggregation. In: Biochimica et Biophysica Acta (BBA) - Biomembranes, 649 (2). pp. 336-342.

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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: Journal Article
Publication: Biochimica et Biophysica Acta (BBA) - Biomembranes
Publisher: Elsevier Science
Additional Information: Copyright of this article belongs to Elsevier Science.
Department/Centre: Division of Biological Sciences > Molecular Biophysics Unit
Date Deposited: 03 Sep 2009 16:56
Last Modified: 19 Sep 2010 05:43
URI: http://eprints.iisc.ac.in/id/eprint/22836

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