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Proteolytic stability of beta-peptide bonds probed using quenched fluorescent substrates incorporating a hemoglobin
Hosahudya N Gopi1, Gudihal Ravindra, Prajna P Pal
1Molecular Biophysics Unit, Indian Institute of Science, Bangalore 560 012, India.
FEBS Letters
|February 1, 2003
Abstract:
A set of designed internally quenched fluorescence peptide substrates has been used to probe the effects of insertion of beta-peptide bonds into peptide sequences. The test sequence chosen corresponds to a proteolytically susceptible site in hemoglobin alpha-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.