Biologically potent analogues of salmon calcitonin which do not contain an N-terminal disulfide-bridged ring structure.
Biologically potent analogues of salmon calcitonin which do not contain an N-terminal disulfide-bridged ring structure.
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鲑鱼降钙素的生物有效类似物，不含 N 末端二硫桥环结构。
DOI：
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发表时间：
1987
期刊：
影响因子：
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通讯作者：
Alan R. Stafford
中科院分区：
文献类型：
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作者：
Ronald C. Orlowski;R. Epand;Alan R. Stafford
鲑鱼降钙素（sCT）的1和7位半胱氨酸残基之间形成的二硫键不是生物活性所必需的。类似物[Ala 1，7]sCT、[AcmCys 1，7]sCT和[AmcCys 1，Ala 7]sCT（AcmC = S-乙酰氨基-甲基半胱氨酸）是线性序列，其在完整大鼠中保留完全的低钙活性和激活大鼠肾膜腺苷酸环化酶的能力。在存在或不存在脂质的情况下，这些肽在水溶液中的二级结构不会受到二硫环打开的极大干扰。与鲑鱼降钙素相反，在人降钙素中用AcmCys取代Cys导致低钙活性大大降低，但肽激活肾腺苷酸环化酶的能力没有损失。因此，体外激活腺苷酸环化酶的人降钙素类似物并不总是与体内低血钙的效力。
The disulfide bridge formed between the cysteine residues at positions 1 and 7 of salmon calcitonin (sCT) is not required for biological activity. The analogues [Ala1,7]sCT,[AcmCys1,7]sCT and [AmcCys1,Ala7]sCT (AcmC = S-acetamido-methylcysteine) are linear sequences which retain full hypocalcemic activity in the intact rat and ability to activate adenylate cyclase of rat renal membranes. The secondary structure of these peptides in aqueous solution in the presence or absence of lipid is not greatly perturbed by the opening of the disulfide ring. In contrast with salmon calcitonin, substitution of Cys by AcmCys in human calcitonin results in greatly reduced hypocalcemic activity but no loss in the ability of the peptide to activate renal adenylate cyclase. Thus in vitro activation of adenylate cyclase by human calcitonin analogues is not always correlated with in vivo hypocalcemic potency.