CAJ | 학술논문

为了研究基于Zn2+-二甲基吡啶胺及胍羰基吡咯基团的配位型受体ZnDpaG与磷酸化肽的相互作用机制,选取具有不同序列的磷酸化肽作用模型,采用等温滴定微量热法考察了ZnDpaG与磷酸化肽的结合常数,研究了模型肽中磷酸基团的数量、密度及位置等因素对多肽与受体间结合强度的影响。结果表明, ZnDpaG受体对双磷酸化肽结合能力显著高于单磷酸化肽,其结合常数可提高10~40倍,2个磷酸基团的距离越近,结合作用越强；而磷酸基团的位置显著影响受体与单磷酸化肽的结合强度。本研究结果为进一步优化磷酸化肽受体结构设计,实现肽与受体间高选择性识别提供了一定的理论依据。
위료연구기우Zn2+-이갑기필정알급고탄기필각기단적배위형수체ZnDpaG여린산화태적상호작용궤제,선취구유불동서렬적린산화태작용모형,채용등온적정미량열법고찰료ZnDpaG여린산화태적결합상수,연구료모형태중린산기단적수량、밀도급위치등인소대다태여수체간결합강도적영향。결과표명, ZnDpaG수체대쌍린산화태결합능력현저고우단린산화태,기결합상수가제고10~40배,2개린산기단적거리월근,결합작용월강；이린산기단적위치현저영향수체여단린산화태적결합강도。본연구결과위진일보우화린산화태수체결구설계,실현태여수체간고선택성식별제공료일정적이론의거。
Study on interaction mechanism between synthetic receptor and phosphorylated peptides is of great importance for phophopeptide enrichment and early disease-detection. In this study, association between Zn2+- coordination type synthetic receptor and some model phosphorylated peptides was studied, the receptor con- tains Zn2+-dipicolylamine and guanidiniocarbonyl pyrrole tethered by hydrophobic spacer. Isothermal titration calorimetry was used to elucidate the association thermodynamics. The receptor displayed higher affinity to bis- phosphorylated peptides in comparison with mono-phosphorylated peptides, and the association constant was 10—40 times higher for bis-phosphorylated peptides than that of mono-phosphorylated peptides. Space be- tween the two phosphate groups showed great influence on the association, i. e. association constant remar- kably decreased as the space increased. For mono-phosphorylated peptides, the position of phosphate in the sequence affected the affinity. The results are expected to provide insights into the principle for the design of receptor for peptides.