Design, synthesis, and characterization of a model peptide having potent calcitonin-like biological activity: implications for calcitonin structure/activity.
Design, synthesis, and characterization of a model peptide having potent calcitonin-like biological activity: implications for calcitonin structure/activity.
复制标题
具有有效降钙素样生物活性的模型肽的设计、合成和表征：对降钙素结构/活性的影响。
作者：
G. Moe;E. Kaiser
降钙素类似物 MCT-II 具有从残基 8 到残基 22 形成两亲性 α 螺旋的潜力，并且在螺旋的疏水面上具有连续的脂肪族亮氨酸侧链表面，已对其物理和生物学特性进行了表征。该肽表现出的特性，包括在微摩尔浓度范围内的自缔合，伴随着α螺旋结构百分比的增加，在空气-水界面形成稳定的单层，以及吸附到鸡蛋卵磷脂单双层囊泡的表面，表明MCT-II可以很容易地形成两亲性α螺旋结构。尽管 MCT-II 与残基 8 至残基 22 的任何特定天然类似物具有最小的序列同源性，但它具有与鲑鱼降钙素 I 相似的生物活性，可与脑和肾膜中的受体结合、激活腺苷酸环化酶以及体内低钙效力。因此，MCT-II 的两亲性 α 螺旋结构对于与降钙素受体的结合非常重要。同样明显的是，天然降钙素的疏水面（位置 15）上常见的亲水残基并不是高生物活性所必需的。（摘要截断为 250 字）
A calcitonin analogue, MCT-II, having the potential to form an amphiphilic alpha-helix from residue 8 to residue 22 with a continuous surface of aliphatic leucine side chains on the hydrophobic face of the helix has been synthesized, and its physical and biological properties have been characterized. Properties exhibited by this peptide, including self-association in the micromolar concentration range with a concomitant increase in the percentage of alpha-helical structure, formation of stable monolayers at the air-water interface, and adsorption to the surface of egg lecithin single-bilayer vesicles, demonstrate that MCT-II can readily form an amphiphilic alpha-helical structure. Though MCT-II has minimal sequence homology to any particular natural analogue from residue 8 to residue 22, it has biological activity similar to that of salmon calcitonin I for receptor binding in brain and kidney membranes, for activation of adenylate cyclase, and in hypocalcemic potency in vivo. The amphiphilic alpha-helical structure of MCT-II, therefore, is important for binding to calcitonin receptors. It is also apparent that a hydrophilic residue commonly occurring on the hydrophobic face (position 15) in the natural calcitonins is not required for high biological activity.(ABSTRACT TRUNCATED AT 250 WORDS)
影响因子：
56.9
作者：
KAISER, ET;KEZDY, FJ
通讯作者：
KEZDY, FJ
单层囊泡中磷脂酶 A2 催化卵磷脂酰胆碱水解的动力学。
DOI：
--
发表时间：
1981
期刊：
The Journal of biological chemistry
影响因子：
--
作者：
Kupferberg,JP;Yokoyama,S;Kézdy,FJ
通讯作者：
Kézdy,FJ