Schiller P W, Maziak L, Nguyen T M, Godin J, Garcia R, De Léan A, Cantin M
Biochem Biophys Res Commun. 1985 Sep 30;131(3):1056-62. doi: 10.1016/0006-291x(85)90197-4.
A linear fragment of the atrial natriuretic factor, ANF(106-125), unable to form an intramolecular cystine bridge, was synthesized by the solid-phase method. The fragment showed smooth muscle relaxant activity in the rabbit aorta and chick rectum assays, an inhibitory effect on aldosterone secretion from bovine adrenal zona glomerulosa cells, and had affinity for specific ANF receptors located in zona glomerulosa cell membranes. The potency of ANF(106-125) in these four assay systems was about two to three orders of magnitude lower than that of ANF(103-125) which contains the intact cyclic structure. The obtained results indicate that the disulfide linkage stabilizes the bioactive conformation of ANF peptides but is not an absolute requirement for biological activity.
通过固相法合成了心房利钠因子线性片段ANF(106 - 125)，该片段无法形成分子内胱氨酸桥。在兔主动脉和鸡直肠实验中，该片段表现出平滑肌舒张活性，对牛肾上腺球状带细胞的醛固酮分泌有抑制作用，并且对位于球状带细胞膜上的特定心房利钠因子受体具有亲和力。在这四个实验系统中，ANF(106 - 125)的效力比含有完整环状结构的ANF(103 - 125)低约两到三个数量级。所得结果表明，二硫键可稳定心房利钠因子肽的生物活性构象，但并非生物活性的绝对必要条件。
