The conformation of angiotensin II. II. The rates of peptide NH exchange with solvent for [Asn1, Val5]angiotensin II, angiotensin III and saralasin

Robert E. Lenkinski; Richard L. Stephens; N. Rama Krishna

doi:10.1016/0005-2795(81)90076-3

The conformation of angiotensin II. II. The rates of peptide NH exchange with solvent for [Asn¹, Val⁵]angiotensin II, angiotensin III and saralasin

Robert E. Lenkinski, Richard L. Stephens, N. Rama Krishna

Research output: Contribution to journal › Article › peer-review

22 Scopus citations

Abstract

The amide hydrogen exchange rates in H₂O of two angiotensin agonists (angiotensinamide and angiotensin III) and one angiotensin antagonist (saralasin) have been measured at room temperature by the transfer of solvent saturation method. The NH of His⁶ is observed to exchange more slowly than predicted for all three peptides, suggesting that it is a participant in an intramolecular hydrogen bond. The NH-C^αH¹H-NMR coupling constants are measured and found to be constant over the pH range of 5.0 to 6.5. The results are compared with those previously obtained for human angiotensin II and interpreted in terms of a dominant three-dimensional structure common to all four molecules. Two models for this structure are evaluated using the observed NH-C^αH coupling constants and the reported activity of conformationally restrained derivatives.

Original language	English (US)
Pages (from-to)	157-167
Number of pages	11
Journal	BBA - Protein Structure
Volume	667
Issue number	1
DOIs	https://doi.org/10.1016/0005-2795(81)90076-3
State	Published - Jan 30 1981

Keywords

Amide hydrogen exchange rate
Angiotensin
NMR
Saralasin

ASJC Scopus subject areas

Medicine(all)

Access to Document

10.1016/0005-2795(81)90076-3

Cite this

@article{611c8891eff74f4990d6278557f0b042,

title = "The conformation of angiotensin II. II. The rates of peptide NH exchange with solvent for [Asn1, Val5]angiotensin II, angiotensin III and saralasin",

abstract = "The amide hydrogen exchange rates in H2O of two angiotensin agonists (angiotensinamide and angiotensin III) and one angiotensin antagonist (saralasin) have been measured at room temperature by the transfer of solvent saturation method. The NH of His6 is observed to exchange more slowly than predicted for all three peptides, suggesting that it is a participant in an intramolecular hydrogen bond. The NH-CαH 1H-NMR coupling constants are measured and found to be constant over the pH range of 5.0 to 6.5. The results are compared with those previously obtained for human angiotensin II and interpreted in terms of a dominant three-dimensional structure common to all four molecules. Two models for this structure are evaluated using the observed NH-CαH coupling constants and the reported activity of conformationally restrained derivatives.",

keywords = "Amide hydrogen exchange rate, Angiotensin, NMR, Saralasin",

author = "Lenkinski, {Robert E.} and Stephens, {Richard L.} and {Rama Krishna}, N.",

note = "Funding Information: The NMR experiments described in this report were performed at the NMR Core Facility in the Comprehensive Cancer Center of the University of Alabama in Birmingham operated under a grant from the U.S. Public Health Service CA-13148 (John R. Durant, M.D.). This work was supported by a grant from the U.S. Public Health Service AM-21980 (R.E.L.). This work was also supported in part by NIH grant GM-25219 (N.R.K.) and by a Postdoctoral Fellowship of the National Library of Medicine, U.S. Public Health Service grant LM 07015-03 (R.L.S.).",

year = "1981",

month = jan,

day = "30",

doi = "10.1016/0005-2795(81)90076-3",

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T1 - The conformation of angiotensin II. II. The rates of peptide NH exchange with solvent for [Asn1, Val5]angiotensin II, angiotensin III and saralasin

AU - Lenkinski, Robert E.

AU - Stephens, Richard L.

AU - Rama Krishna, N.

N1 - Funding Information: The NMR experiments described in this report were performed at the NMR Core Facility in the Comprehensive Cancer Center of the University of Alabama in Birmingham operated under a grant from the U.S. Public Health Service CA-13148 (John R. Durant, M.D.). This work was supported by a grant from the U.S. Public Health Service AM-21980 (R.E.L.). This work was also supported in part by NIH grant GM-25219 (N.R.K.) and by a Postdoctoral Fellowship of the National Library of Medicine, U.S. Public Health Service grant LM 07015-03 (R.L.S.).

PY - 1981/1/30

Y1 - 1981/1/30

N2 - The amide hydrogen exchange rates in H2O of two angiotensin agonists (angiotensinamide and angiotensin III) and one angiotensin antagonist (saralasin) have been measured at room temperature by the transfer of solvent saturation method. The NH of His6 is observed to exchange more slowly than predicted for all three peptides, suggesting that it is a participant in an intramolecular hydrogen bond. The NH-CαH 1H-NMR coupling constants are measured and found to be constant over the pH range of 5.0 to 6.5. The results are compared with those previously obtained for human angiotensin II and interpreted in terms of a dominant three-dimensional structure common to all four molecules. Two models for this structure are evaluated using the observed NH-CαH coupling constants and the reported activity of conformationally restrained derivatives.

AB - The amide hydrogen exchange rates in H2O of two angiotensin agonists (angiotensinamide and angiotensin III) and one angiotensin antagonist (saralasin) have been measured at room temperature by the transfer of solvent saturation method. The NH of His6 is observed to exchange more slowly than predicted for all three peptides, suggesting that it is a participant in an intramolecular hydrogen bond. The NH-CαH 1H-NMR coupling constants are measured and found to be constant over the pH range of 5.0 to 6.5. The results are compared with those previously obtained for human angiotensin II and interpreted in terms of a dominant three-dimensional structure common to all four molecules. Two models for this structure are evaluated using the observed NH-CαH coupling constants and the reported activity of conformationally restrained derivatives.

KW - Amide hydrogen exchange rate

KW - Angiotensin

KW - NMR

KW - Saralasin

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