Resent studies on analogues and homologues of angiotensin I, the pressor octapeptide L-aspart1-L-arginyl-L-valyl-L-tyrosyl-L-histidyl-L-prolyl-L-phenylalanine, have shown the two amino acids with aomatic rings are important to biological activity.
Rem...
Resent studies on analogues and homologues of angiotensin I, the pressor octapeptide L-aspart1-L-arginyl-L-valyl-L-tyrosyl-L-histidyl-L-prolyl-L-phenylalanine, have shown the two amino acids with aomatic rings are important to biological activity.
Removal of the aromatic ring of phenylalanine greatly reduced pressor activity. The peptide without the phenolic hydroxy group of tyrosine, phenylalanine angiotensin, has only 2 to 10% of the activity of the parent octapeptide.
The two aromatic side gropes are positioned, very close to each other in a conformation recently suggested for angiotensin I.