Bajusz S, Fauszt I, Németh K, Barabás E, Juhász A, Patthy M
Institute for Drug Research, Budapest, Hungary.
Bioorg Med Chem Lett. 1998 Jun 16;8(12):1477-82. doi: 10.1016/s0960-894x(98)00244-3.
Inhibition of interleukin-1 beta converting enzyme (ICE), apopain, papain, thrombin and trypsin with substrate like peptidyl L- and D-alpha-aldehydes and their L-beta-homo-aldehyde analogues was investigated. The L-beta-homo-aspartals appear to be specific inhibitors for ICE and its homologues; the other enzymes were not inhibited with such L-beta-homo aldehydes. Papain shows tolerance for D-residues at P1 depending on their chiral stability.
研究了用肽基L-和D-α-醛及其L-β-高醛类似物等底物对白细胞介素-1β转化酶(ICE)、凋亡蛋白酶、木瓜蛋白酶、凝血酶和胰蛋白酶的抑制作用。L-β-高天冬氨酸似乎是ICE及其同源物的特异性抑制剂;其他酶不受此类L-β-高醛的抑制。木瓜蛋白酶对P1处的D-残基具有耐受性,这取决于它们的手性稳定性。