Alamethicin and synthetic peptide fragments as uncouplers of mitochondrial oxidative phosphorylation. Effect of chain length and change

Mathew, M. K. ; Nagaraj, R. ; Balaram, P. (1981) Alamethicin and synthetic peptide fragments as uncouplers of mitochondrial oxidative phosphorylation. Effect of chain length and change Biochemical and Biophysical Research Communications, 98 (2). pp. 548-555. ISSN 0006-291X

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Official URL: http://linkinghub.elsevier.com/retrieve/pii/000629...

Related URL: http://dx.doi.org/10.1016/0006-291X(81)90875-5

Abstract

Alamethicin, its derivatives and some synthetic fragments have been shown to be uncouplers of oxidative phosphorylation in rat liver mitochondria. A minimum peptide chain length of 13 residues is necessary for this activity. Peptide esters are more efficient uncouplers than the corresponding peptide acids. Esterification of the Glu(18) γ-COOH group in alamethicin does not diminish uncoupling activity. The structural requirements for uncoupling activity parallel those determined for ionophoretic action in small, unilamellar liposomes.

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