Conformations in solution of angiotensin II, and its 1-7 and 1-6 fragments.
High-resolution proton spectra at 620 MHz of human angiotensin II (1-8), angiotensin II (1-7), and angiotensin II (1-6) have been obtained in aqueous solution at acidic pH, and in dimethylsulfoxide solution. Complete chemical shift assignments for all three angiotensin peptides were made based on two-dimensional (2D) correlated spectroscopy and 2D-CA-MELSPIN spectra. Based on the measured values of 3JHNCH, the pattern of observed transverse Overhauser effects, and side-chain coupling constants, it is concluded that all three analogues exist in H2O or DMSO-d6 as a mixture of conformers that is largely extended, with negligible content of folded structures, such as beta-turns, gamma-turns, or helix content. The results fit well with those of Nikiforovich et al.
Cushman
J A
JA
Department of Chemistry, Carnegie Mellon University, Pittsburgh, Pennsylvania 15213.
Mishra
P K
PK
Bothner-By
A A
AA
Khosla
M S
MS
D000804:Angiotensin II / Q000737:chemistry*; D006801:Humans; D009682:Magnetic Resonance Spectroscopy; D011487:Protein Conformation; D012996:Solutions
D012996:Solutions; D000804:Angiotensin II