【摘 要】
：
N-terminal analogs of dermorphin Tyr-D-Ala-Phe-Gly-Tyr-Pro-Ser-NH2 and deltorphin Tyr-D-Ala-Phe-Asp/Glu-Val-Val-Gly-NH2,viz.Tyr-D-Arg-Phe-Lys-NH2 (DALDA) an
【机 构】
：
UniversityofGda(n)skPoland
【出 处】
：
2008中国深圳蛋白质和多肽科学大会
论文部分内容阅读
N-terminal analogs of dermorphin Tyr-D-Ala-Phe-Gly-Tyr-Pro-Ser-NH2 and deltorphin Tyr-D-Ala-Phe-Asp/Glu-Val-Val-Gly-NH2,viz.Tyr-D-Arg-Phe-Lys-NH2 (DALDA) and [Dmt1]DALDA (Dmt=2"27,6"27-dimethyltyrosine) are the most potent and selective μ-agonists reported to date.A succesful strategy to understand molecular basis of opioid bioactivity and selectivity is a design of analogs with major conformational restraints imposed by cyclization.Here we describe the following types of deltorphin analogs,restrained by merging the side chains of residues 2 and 4:(1) The heptapeptide amides incorporating dibasic amino acid residues (Lys,Orn,Dab,Dap) in positions 2 and 4,cycled by an urea bridge,referred to their N-terminal tetrapeptide counterparts; (2) The tetrapeptide amide Tyr-c[D-Cys-Phe-Cys]NH2,constrained via an SγS "γ disulphide between Cys-2 and Cys-4,and its dicarba analogs,both CγCr-saturated and-olefinic ones.
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