Gopi, Hosahudya N. ; Ravindra, Gudihal ; Pal, Prajna P. ; Pattanaik, Priyaranjan ; Balaram, Hemalatha ; Balaram, Padmanabhan (2003) Proteolytic stability of beta-peptide bonds probed using quenched fluorescent substrates incorporating a hemoglobin cleavage site FEBS Letters, 535 (1-3). pp. 175-178. ISSN 0014-5793
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Official URL: http://www.sciencedirect.com/science/article/pii/S...
Related URL: http://dx.doi.org/10.1016/S0014-5793(02)03885-1
Abstract
A set of designed internally quenched fluorescence peptide substrates has been used to probe the effects of insertion of β-peptide bonds into peptide sequences. The test sequence chosen corresponds to a proteolytically susceptible site in hemoglobin α-chain, residues 32–37. Fluorescence and mass spectral measurements demonstrate that the insertion of an β-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: | Article |
|---|---|
| Source: | Copyright of this article belongs to Elsevier Science. |
| Keywords: | β-Peptides; Fluorescent Protease Substrate; Fluorescence Resonance Energy Transfer; Mass Spectrometry; Proteolytic Stability; Hemoglobin |
| ID Code: | 94674 |
| Deposited On: | 18 Oct 2012 07:39 |
| Last Modified: | 18 Oct 2012 07:39 |
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