Production of an atrial natriuretic peptide variant that is specific for type A receptor.

摘要: Receptor-specific variants of atrial natriuretic peptide (ANP) were selected from libraries filamentous phage particles that displayed single copies random ANP mutants fused to gene III protein. These differentially by binding immobilized receptor A (NPR-A) over competing C (NPR-C) in solution. This method also with improved secretion expression Escherichia coli. Several the identified mutations combined produce an efficiently expressed analog was as potent wild-type stimulating NPR-A guanylyl cyclase activity but resistant inactivation mediated NPR-C. Such NPR-A-selective analogs should be useful for correlating various activities relevant and may more therapeutics targeting NPR-A.