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Structure formation in short designed peptides probed by proteolytic cleavage

Saikumari, Yegnisettipalli K and Ravindra, Gudihal and Balaram, Padmanabhan (2006) Structure formation in short designed peptides probed by proteolytic cleavage. In: Protein and Peptide Letters, 13 (5). pp. 471-476.

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Abstract

The formation of local structure, in short peptides has been probed by examining cleavage patterns and rates of proteolysis of designed sequences with a high tendency to form β-hairpin structures. Three model sequences which bear fluorescence donor and acceptor groups have been investigated: Dab-Gaba-Lys-Pro-Leu-Gly-Lys-Val-Xxx-Yyy-Glu-Val-Ala-Ala-Cys-Lys-NH2 ï EDANS Xxx-Yyy: Peptide 1=DPro-LPro, Peptide 2=DPro-Gly, Peptide 3=Leu-Ala Fluorescence resonance energy transfer (FRET) provides a convenient probe for peptide cleavage. MALDI mass spectrometry has been used to probe sites of cleavage and CD spectroscopy to access the overall backbone conformation using analog sequences, which lack strongly absorbing donor and acceptor groups. The proteases trypsin, subtilisin, collagenase, elastase, proteinase K and thermolysin were used for proteolysis and the rates of cleavage determined. Peptide 3 is the most susceptible to cleavage by all the enzymes except thermolysin, which cleaves all three peptides at comparable rates. Peptides 1 and 2 are completely resistant to the action of trypsin, suggesting that β-turn formation acts as a deterrent to proteolytic cleavage.

Item Type: Journal Article
Additional Information: Copy right of this article belongs to Bentham Science Publishers.
Keywords: Fluorescent protease substrate; fluorescence resonance energy transfer; mass spectrometry; circular dichroism; β-hairpin peptide; β- turn; proteases
Department/Centre: Division of Biological Sciences > Molecular Biophysics Unit
Date Deposited: 30 Apr 2010 04:48
Last Modified: 19 Sep 2010 06:01
URI: http://eprints.iisc.ernet.in/id/eprint/27398

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