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Amphipathic helical potency and its relationship to the biological activity of synthetic calcitonin derivatives

机译:两性疗法循环效力及其与合成降钙素衍生物生物活性的关系

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Three structural regions: a seven-residue cyclic segment at the N-terminus formed by a disulfide bond between cysteines at positions 1 and 7, an amphipathic alpha -helix from residue 8 tothe helix-breaking proline at position 23, and a hydrophilic random coil segment from residue 23 to the C-terminal proline amide may be important in the biological activity of calcitonin [1]. Four salmon calcitonin (sCT) analogues were designe,d synthesized and their conformational properties were studied by Fourier-transform infrared (FTIR) spectroscopy and circular dichroism (CD).
机译:三个结构区域:通过在位置1和7的半胱氨酸之间的二硫键形成的N-末端的七残基循环区段,来自残留物8的两亲α-helix在第23位,螺旋破裂脯氨酸和亲水性无规管将残余物23与C-末端脯氨酸酰胺的链段在降钙素中的生物活性中可能是重要的[1]。四种鲑鱼降钙素(SCT)类似物是设计,D合成的D合成,并通过傅里叶变换红外(FTIR)光谱和圆形二色性(CD)研究了它们的构象性能。

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