Fluorescent Hydrophobic Peptide Fragments of Emerimicin. Models for the Study of Peptide Aggregation and Interactions with Lipids and Proteins

Nagaraj, R and Balaram, P (1979) Fluorescent Hydrophobic Peptide Fragments of Emerimicin. Models for the Study of Peptide Aggregation and Interactions with Lipids and Proteins. In: Biochemical and Biophysical Research Communications, 89 (4). pp. 1041-1049.

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Abstract

The fluorescent amino terminal fragments of emerimicin, dansyl-Phe-Aib-Aib-OMe, dansyl-Phe-Aib-Aib-Aib-Val-OMe and dansyl-Phe-Aib-Aib-Aib-Val-Gly-Leu-Aib-Aib-OMe and the corresponding peptide acids have been synthesised. The nonapeptide ester aggregates at concentrations greater than 8 \mu M whereas the tri and pentapeptide esters do not. The peptide acids also do not aggregate. The esters bind to lipid dispersions with the largest changes in fluorescence observed for the nonapeptide, whereas the acids interact very weakly. The acids show changes in fluorescence in the presence of bovine serum albumin, in contrast to the esters with the shorter peptides showing larger effects.

Item Type:	Journal Article
Publication:	Biochemical and Biophysical Research Communications
Publisher:	Elsevier
Additional Information:	Copyright for this article belongs to Elsevier Science Ltd.
Department/Centre:	Division of Biological Sciences > Molecular Biophysics Unit
Date Deposited:	18 Apr 2005
Last Modified:	19 Sep 2010 04:18
URI:	http://eprints.iisc.ac.in/id/eprint/3081

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