Department of Chemistry, Yerevan State University, 0025, Yerevan, Armenia.
Institute of Pharmacy, Yerevan State University, 0025, Yerevan, Armenia.
J Fluoresc. 2020 Mar;30(2):229-233. doi: 10.1007/s10895-020-02504-3. Epub 2020 Feb 12.
The interaction of (2R, 3S)-hydroxyleucine (trypsin inhibitor) and β-hydroxyvaline with trypsin has been studied by the steady-state fluorescence spectroscopy. The analysis of fluorescence spectra has revealed the mechanism of binding of these nonprotein amino acids to trypsin. According to the docking (2R, 3S)-hydroxyleucine form hydrogen bonds with trypsin having little effect on tryptophan and tyrosine residues in enzyme molecule. The results obtained in this study indicate that fluorescence of trypsin is quenched at high concentrations of amino acids. Thus fluorescence spectra analysis confirms data obtained by molecular docking.
（2R，3S）-羟基亮氨酸（胰蛋白酶抑制剂）和β-羟基缬氨酸与胰蛋白酶的相互作用已通过稳态荧光光谱法进行了研究。荧光光谱分析揭示了这些非蛋白氨基酸与胰蛋白酶结合的机制。根据对接，（2R，3S）-羟基亮氨酸与胰蛋白酶形成氢键，对酶分子中的色氨酸和酪氨酸残基影响很小。本研究的结果表明，在氨基酸浓度较高时，胰蛋白酶的荧光被猝灭。因此，荧光光谱分析证实了分子对接获得的数据。
