1H NMR Conformational Studies in Water of Angiotensin II Analogues Modified at the N- and C-Termini: Interactions of the Aromatic Side Chains and Folding of the N-Terminal Domain

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Title:1H NMR Conformational Studies in Water of Angiotensin II Analogues Modified at the N- and C-Termini: Interactions of the Aromatic Side Chains and Folding of the N-Terminal Domain
Creators:
Hondrelis, John
Matsoukas, John
Agelis, George
Cordopatis, Paul
Zhou, Ning
Vogel, Hans
Moore, Graham J.
Journal or Publication Title:
Collection of Czechoslovak Chemical Communications, 59, 11, pp. 2523-2532

Abstract

<p>The conformation of [Sar<sup>1</sup>]angiotensin <i>II</i> in water at neutral pH has been examined by proton magnetic resonance spectroscopy at 400 MHz and in particular by comparing its <sup>1</sup>H NMR spectral data with those of analogues modified at positions 1,4 and 6, namely [Sar<sup>1</sup>,Cha<sup>8</sup>]ANGII, [Des Asp<sup>1</sup>,Cha<sup>8</sup>]ANGII, [Aib<sup>1</sup>,Tyr(Me)<sup>4</sup>]ANGII, [Aib<sup>1</sup>,Tyr(Me)<sup>4</sup>,Ile<sup>8</sup>]ANGII, [N-MeAib<sup>1</sup>,Tyr(Me)<sup>4</sup>]ANGII, [N-MeAib<sup>1</sup>,Tyr(Me)<sup>4</sup>,Ile<sup>8</sup>]ANGII, ANGIII and [Sar<sup>1</sup>,Ile<sup>8</sup>]ANGII. Assignment of all proton resonances in these analogues was made possible by 2D COSY NMR experiments. The H-2 and H-4 protons for the histidine ring in [Sar<sup>1</sup>]ANGII, ANGII and ANGIII were shielded compared with the same protons in [Sar<sup>1</sup>,Ile<sup>8</sup>]ANGII, [Sar<sup>1</sup>,Cha<sup>8</sup>]ANGII and [Des Asp<sup>1</sup>,Cha<sup>8</sup>]ANGII; this shielding effect was not disturbed upon methylation of the tyrosine hydroxyl and/or replacement of residue 1 (sarcosine or aspartic acid) with aminoisobutyric acid (Aib) or <i>N</i>-methyl aminoisobutyric acid (N-MeAib). These data are consistent with our previous suggestion based on NMR studies in neutral DMSO that a characteristic folded conformation for ANGII previously observed in non-polar solvents can also be detected in water at neutral pH, but to a lesser degree.

Title:1H NMR Conformational Studies in Water of Angiotensin II Analogues Modified at the N- and C-Termini: Interactions of the Aromatic Side Chains and Folding of the N-Terminal Domain
Creators:
Hondrelis, John
Matsoukas, John
Agelis, George
Cordopatis, Paul
Zhou, Ning
Vogel, Hans
Moore, Graham J.
Divisions:Life and Chemical Sciences > Institute of Organic Chemistry and Biochemistry > Collection of Czechoslovak Chemical Communications
Journal or Publication Title:Collection of Czechoslovak Chemical Communications
Volume:59
Number:11
Page Range:pp. 2523-2532
ISSN:0010-0765
E-ISSN:1212-6950
Publisher:Institute of Organic Chemistry and Biochemistry
Related URLs:
URLURL Type
http://dx.doi.org/10.1135/cccc19942523UNSPECIFIED
ID Code:671
Item Type:Article
Deposited On:06 Feb 2009 17:02
Last Modified:06 Feb 2009 16:03

Citation

Hondrelis, John; Matsoukas, John; Agelis, George; Cordopatis, Paul; Zhou, Ning; Vogel, Hans; Moore, Graham J. (1994) 1H NMR Conformational Studies in Water of Angiotensin II Analogues Modified at the N- and C-Termini: Interactions of the Aromatic Side Chains and Folding of the N-Terminal Domain. Collection of Czechoslovak Chemical Communications, 59 (11). pp. 2523-2532. ISSN 0010-0765

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