Báo cáo khoa học: Role of hydroxyl group and R/S configuration of isostere in binding properties of HIV-1 protease inhibitors
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The crystal structure of the complex between human immunodeficiency virus type 1 (HIV-1) protease and a peptidomimetic inhibitor of ethyleneamine type has been refined toRfactor of 0.178 with diffraction limit 2.5 A ˚ .The peptidomimetic inhibitor Boc-Phe-Y[CH2CH2 NH]-Phe-Glu-Phe-NH2 (denoted here as OE) contains the ethylene-amine replacement of the scissilepeptidebond. The inhibitor lacks the hydroxyl group which is believed to mimic tetra-hedral transition state of proteolytic reaction and thus is suspected to be necessary for good properties of peptido-mimetic HIV-1 protease inhibitors....
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