Synthesis and biological activity of a linear fragment of the atrial natriuretic factor (ANF).

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.