Abstract
Synthesis of fluorogenic peptide substrate of HIV-1 protease Dns-SQNYPIVWL which corresponds to the pi?7p24 cleavage site forHIV-J protease havebeen performed. This fluorogenic substrate was based onthe fluorescence resonance energy transfer between donor — Trp residue, and acceptor — dansyl group in the intact peptide. Hydrolysis of substrate by recombinant HIV-1 protease resulted in the time-dependent increase ofTrp fluorescence and decrease of dansyl fluorescence measured at 350 and 500 nm, respectively, due to the break of resonance energy transfer between donor and acceptorfluorophors. Hydrolysis of fluoro genic peptide substrate was studied also by reversed phase HPLC and two peptide fragments after cleavage of substrate have been detected. Kinetic constants of hydrolysis for this fluorogenic peptide substrate by HIV-1 protease were calculated from Lineweaver— Burk plots: KM -29pM, kcat - 5.4 s'1 and kcailKM 180 000 hf V і .
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