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.
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|
|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|
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