Proteolytic stability of beta-peptide bonds probed using quenched fluorescent substrates incorporating a hemoglobin cleavage site

Gopi, Hosahudya N and Ravindra, Gudihal and Pal, Prajna P and Pattanaik, Priyaranjan and Balaram, Hemalatha and Balaram, Padmanabhan (2003) Proteolytic stability of beta-peptide bonds probed using quenched fluorescent substrates incorporating a hemoglobin cleavage site. In: FEBS Letters, 535 (1-3). pp. 175-178.

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Abstract

A set of designed internally quenched fluorescence peptide substrates has been used to probe the e¡ects of insertion of beta-peptide bonds into peptide sequences. The test sequence chosen corresponds to a proteolytically susceptible site in hemoglobin K-chain, residues 32-37. Fluorescence and mass spectral measurements demonstrate that the insertion of an beta-residues at the potential cleavage sites completely abolishes the action of proteases; in addition, the rate of cleavage of the peptide bond preceding the site of modification is also considerably reduced.

Item Type:	Journal Article
Publication:	FEBS Letters
Publisher:	Elsevier
Additional Information:	Copyright for this article belongs to Elsevier Science Ltd
Keywords:	Beta-Peptides;Fluorescent protease substrate;Fluorescence resonance energy transfer;Mass spectrometry;Proteolytic stability;Hemoglobin
Department/Centre:	Division of Biological Sciences > Molecular Biophysics Unit
Date Deposited:	03 Aug 2004
Last Modified:	19 Sep 2010 04:14
URI:	http://eprints.iisc.ac.in/id/eprint/1222

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