Synthetic analogues of residues 1-34 of human parathyroid hormone: influence of residue number 1 on biological potency in vitro.
A biologically active tetratriacontapeptide of human parathyroid hormone, hPTH (1-34), has been synthesized together with a series of structural analogues involving changes at the amino-terminal residue. Acetylation of the terminal amino group results in a marked reduction in the biological potency as measured in the in vitro rat renal adenylyl cyclase assay. Deletion of the terminal amino group results in a loss of biological activity. Substitution of the amino-terminal serine residue with glycine gives a lowered potency whereas substitution with alanine results in a 2-5-fold increase in biological activity in the in vitro assay. The results are compared with the findings previously reported for a series of amino-terminal analogues of the bovine PTH 1-34 peptide.
D000262:Adenylyl Cyclases / Q000032:analysis; D000409:Alanine; D000818:Animals; D007668:Kidney / Q000032:analysis; D010281:Parathyroid Hormone / Q000031:analogs & derivatives* / Q000138:chemical synthesis*; D051381:Rats; D012694:Serine; D013329:Structure-Activity Relationship
D010281:Parathyroid Hormone; D012694:Serine; D000262:Adenylyl Cyclases; D000409:Alanine