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Title: NMR study of the possible interaction in solution of angiotensin II with a peptide encoded by angiotensin II complementary RNA

Journal Article · · Proceedings of the National Academy of Sciences of the United States of America; (USA)
;  [1]; ;  [2]
  1. Abbott Labs., Abbott Park, IL (USA)
  2. Univ. of Texas, Austin (USA)

The potential binding of angiotensin II (Asp-Arg-Val-Tyr-Ile-His-Pro-Phe) (AII) to a peptide encoded by its complementary RNA (Lys-Gly-Val-Asp-Val-Try-Ala-Val) (IIA) has been studied by monitoring the {sup 1}H NMR spectrum of IIA in aqueous phosphate or Tris{center dot}HCl buffer ({sup 2}H{sub 2}O) as it is titrated with AII. For molar ratios of AII/IIA ranging from 0.2 to 1.8, the NMR spectra are unchanged as compared to the spectra of the isolated peptides. Based on these findings, the K{sub d} for the putative biomolecular complex of the two peptides under these conditions is calculated to be >10{sup {minus}4} M. This result does not support the suggestion of Elton et al. that AII and IIA engage in high-affinity binding (K{sub d} {approx} 5 {times} 10 {sup {minus}8} M) with each other.

OSTI ID:
6921072
Journal Information:
Proceedings of the National Academy of Sciences of the United States of America; (USA), Vol. 86:24; ISSN 0027-8424
Country of Publication:
United States
Language:
English