AT4 receptor binding characteristics: D-amino acid- and glycine-substituted peptides.
The ability of angiotensin IV (AIV) analogs to compete for [125I]AIV binding in heat-treated bovine adrenal membranes was examined. Angiotensin IV displayed a Ki of 2.63 +/- 0.12 nM. Peptides containing mono-substitutions with glycine or the corresponding D-amino acid in positions one, two, or three possessed K(i)s greater than 100 nM. Conversely, substitutions at positions four, five, and six produced peptides with Kis less than 8 nM. These data suggest that the N-terminal domains of the AIV peptide are critical for receptor binding, while the C-terminal domains play a less decisive role in receptor specificity.
Sardinia
M F
MF
Department of Veterinary and Comparative Anatomy, Pharmacology, and Physiology, Washington State University, Pullman 99164-6520.
Hanesworth
J M
JM
Krebs
L T
LT
Harding
J W
JW
D000595:Amino Acid Sequence; D000596:Amino Acids; D000804:Angiotensin II / Q000031:analogs & derivatives* / Q000378:metabolism; D000818:Animals; D002417:Cattle; D005998:Glycine; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry / Q000378:metabolism*; D011945:Receptors, Angiotensin / Q000378:metabolism*; D013329:Structure-Activity Relationship
D000596:Amino Acids; D010455:Peptides; D011945:Receptors, Angiotensin; D000804:Angiotensin II; C012877:angiotensin II, des-Asp(1)-des-Arg(2)-Ile(5)-; D005998:Glycine