Zhorov B S, Ananthanarayanan V S
Department of Biochemistry, McMaster University, Hamilton, Ontario, Canada.
J Biomol Struct Dyn. 1995 Aug;13(1):1-13. doi: 10.1080/07391102.1995.10508817.
Based on our earlier proposal on the role of Ca2+ in ligand-receptor recognition and the demonstration of the similarity of the Ca(2+)-bound forms of Met-enkephalin and morphine (Zhorov, B.S. and Ananthanarayanan, V.S., FEBS Lett. 354, 131-134 (1994)) we have undertaken the conformational analysis of a series of the Ca(2+)-bound opioid peptides aiming to find their conformations matching Ca(2+)-bound morphine. A Monte Carlo-with-energy-minimization method was used to calculate 14 opioid peptides in the presence of Ca2+. Low-energy conformations of the Ca2+ complexes of peptides with high mu-affinity were found to resemble closely morphine-Ca2+ complex. In contrast, the Ca2+ complexes of peptides with low mu-affinity did not. The results are relevant for understanding the structure-activity relations of opioid receptor ligands.
基于我们之前关于Ca2+在配体-受体识别中的作用的提议，以及甲硫氨酸脑啡肽和吗啡的Ca(2+)结合形式的相似性证明（佐罗夫，B.S.和阿南塔拉亚南，V.S.，《欧洲生物化学学会联合会快报》354，131 - 134（1994）），我们对一系列Ca(2+)结合的阿片肽进行了构象分析，旨在找到与Ca(2+)结合的吗啡相匹配的构象。采用蒙特卡罗-能量最小化方法在Ca2+存在的情况下计算了14种阿片肽。发现具有高μ亲和力的肽的Ca2+复合物的低能量构象与吗啡-Ca2+复合物非常相似。相比之下，具有低μ亲和力的肽的Ca2+复合物则不然。这些结果对于理解阿片受体配体的构效关系具有重要意义。
