Proteolytic stability of β‐peptide bonds probed using quenched fluorescent substrates incorporating a hemoglobin cleavage site

FEBS Letters

Balaram, Padmanabhan²  Pal, Prajna P.²  Pattanaik, Priyaranjan¹  Ravindra, Gudihal²  Balaram, Hemalatha¹  Gopi, Hosahudya N.² 

[1] Molecular Biology and Genetics Unit, Jawaharlal Nehru Center for Advanced Scientific Research, Bangalore 560 064, India;Molecular Biophysics Unit, Indian Institute of Science, Bangalore 560 012, India

关键词: β-Peptides;    Fluorescent protease substrate;    Fluorescence resonance energy transfer;    Mass spectrometry;    Proteolytic stability;    Hemoglobin;   

DOI  :  10.1016/S0014-5793(02)03885-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown