Jump to ContentJump to Main Navigation
Show Summary Details
More options …

Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

Editorial Board: Buchner, Johannes / Lei, Ming / Ludwig, Stephan / Sies, Helmut / Thomas, Douglas D. / Turk, Boris / Wittinghofer, Alfred

12 Issues per year


IMPACT FACTOR 2017: 3.022

CiteScore 2017: 2.81

SCImago Journal Rank (SJR) 2017: 1.562
Source Normalized Impact per Paper (SNIP) 2017: 0.705

Online
ISSN
1437-4315
See all formats and pricing
More options …
Volume 387, Issue 4

Issues

Novel ketomethylene inhibitors of angiotensin I-converting enzyme (ACE): inhibition and molecular modelling

Pierre Redelinghuys
  • Division of Medical Biochemistry, Institute of Infectious Disease and Molecular Medicine, University of Cape Town, Observatory 7925, Cape Town, South Africa
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
/ Aloysius T. Nchinda
  • Division of Medical Biochemistry, Institute of Infectious Disease and Molecular Medicine, University of Cape Town, Observatory 7925, Cape Town, South Africa
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
/ Kelly Chibale / Edward D. Sturrock
  • Division of Medical Biochemistry, Institute of Infectious Disease and Molecular Medicine, University of Cape Town, Observatory 7925, Cape Town, South Africa
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
Published Online: 2006-04-11 | DOI: https://doi.org/10.1515/BC.2006.061

Abstract

Inhibition of angiotensin I-converting enzyme (ACE) has become an effective strategy in the treatment of hypertension and cardiovascular disease. Keto-ACE, a previously described C-domain selective ACE inhibitor, was used as the basis for the design, synthesis and molecular modelling of a series of novel ketomethylene derivatives for which ACE inhibition profiles and structural characterisation are reported. K i determinations indicated that the introduction of a bulky aromatic tryptophan at the P2′ position of keto-ACE significantly increased selectivity for the C-domain, while an aliphatic P2 Boc group conferred N-domain selectivity. These data were supported by the potential energies of the compounds docked with the C- and N-domains of ACE.

Keywords: kinetics; molecular modelling; physico-chemical characterisation; protease

About the article

Corresponding author


Received: August 26, 2005

Accepted: January 11, 2006

Published Online: 2006-04-11

Published in Print: 2006-04-01


Citation Information: Biological Chemistry, Volume 387, Issue 4, Pages 461–466, ISSN (Online) 1437-4315, ISSN (Print) 1431-6730, DOI: https://doi.org/10.1515/BC.2006.061.

Export Citation

Citing Articles

Here you can find all Crossref-listed publications in which this article is cited. If you would like to receive automatic email messages as soon as this article is cited in other publications, simply activate the “Citation Alert” on the top of this page.

[1]
Aloysius T. Nchinda, Kelly Chibale, Pierre Redelinghuys, and Edward D. Sturrock
Bioorganic & Medicinal Chemistry Letters, 2006, Volume 16, Number 17, Page 4612
[2]
Jean M. Watermeyer, Wendy L. Kröger, Hester G. O'Neill, B. Trevor Sewell, and Edward D. Sturrock
Biochemical Journal, 2010, Volume 428, Number 1, Page 67
[3]
Yu. E. Elisseeva and E. V. Kugaevskaya
Biochemistry (Moscow) Supplement Series B: Biomedical Chemistry, 2009, Volume 3, Number 3, Page 237
[4]
A.S. Pina and A.C.A. Roque
Journal of Molecular Recognition, 2009, Volume 22, Number 2, Page 162

Comments (0)

Please log in or register to comment.
Log in