Conformational diversity of T-kinin in DMSO, water and HFA

Conformational diversity of T-kinin in DMSO, water and HFA T-kinin (Ile-Ser-BK) is related to BK in its biological profile, but unlike BK, is more resistant to the action of ACE. A detailed NMR and molecular modeling study of T-kinin has been carried out in three diverse media: water (pH 4.0), DMSO- d 6 and HFA solution. In DMSO- d 6 , T-kinin adopts a structure with two tandem β-turns: the first at the mid segment tetrad Pro 4 -Pro 5 -Gly 6 -Phe 7 (type I) and the C-terminal end Ser 8 -Pro 9 -Phe 10 -Arg 11 harbors the second turn (also type I). While the first β-turn is lost in presence of water, the second persists. In HFA, NMR reveals a α-helix like structure spanning residues Arg 3 to Arg 11 . Structures with cis peptide bonds (XX-Pro) have been observed for T-kinin in DMSO- d 6 but not in water and HFA. Differences in the structures of BK and T-kinin in water may explain their susceptibility/resistance to the action of ACE. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png European Journal of Medicinal Chemistry Elsevier

Conformational diversity of T-kinin in DMSO, water and HFA

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Publisher
Elsevier
Copyright
Copyright © 2002 Éditions scientifiques et médicales Elsevier SAS
ISSN
0223-5234
eISSN
1768-3254
D.O.I.
10.1016/S0223-5234(01)01323-X
Publisher site
See Article on Publisher Site

Abstract

T-kinin (Ile-Ser-BK) is related to BK in its biological profile, but unlike BK, is more resistant to the action of ACE. A detailed NMR and molecular modeling study of T-kinin has been carried out in three diverse media: water (pH 4.0), DMSO- d 6 and HFA solution. In DMSO- d 6 , T-kinin adopts a structure with two tandem β-turns: the first at the mid segment tetrad Pro 4 -Pro 5 -Gly 6 -Phe 7 (type I) and the C-terminal end Ser 8 -Pro 9 -Phe 10 -Arg 11 harbors the second turn (also type I). While the first β-turn is lost in presence of water, the second persists. In HFA, NMR reveals a α-helix like structure spanning residues Arg 3 to Arg 11 . Structures with cis peptide bonds (XX-Pro) have been observed for T-kinin in DMSO- d 6 but not in water and HFA. Differences in the structures of BK and T-kinin in water may explain their susceptibility/resistance to the action of ACE.

Journal

European Journal of Medicinal ChemistryElsevier

Published: Feb 1, 2002

References

  • Eur. J. Pharmacol
    Lopes, P.; Couture, R.
  • J. Mol. Biol.
    Qian, N.; Sejnowski, T.

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