Mathew, MK and Nagarajan, R and Balaram, P (1981) Alamethicin and synthetic peptide fragments as uncouplers of mitochondrial oxidative phosphorylation. Effect of chain length and change. In: Biochemical and Biophysical Research Communications, 98 (2). pp. 548-555.
PDF
33.pdf - Published Version Restricted to Registered users only Download (428kB) | Request a copy |
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. Aib, α-aminoisobutyric acid; Z, benzyloxycarbonyl; OMe, methyl ester; OBz, benzyl ester; Ac, acetyl; CTC, chlortetracycline.
Item Type: | Journal Article |
---|---|
Publication: | Biochemical and Biophysical Research Communications |
Publisher: | Elsevier Science |
Additional Information: | Copyright of this article belongs to Elsevier Science. |
Department/Centre: | Division of Biological Sciences > Molecular Biophysics Unit |
Date Deposited: | 18 Aug 2009 04:35 |
Last Modified: | 19 Sep 2010 05:41 |
URI: | http://eprints.iisc.ac.in/id/eprint/22358 |
Actions (login required)
View Item |