Probing the importance of spacial and conformational domains in captopril analogs for angiotensin converting enzyme activity

S Hanessian; U Reinhold; M Saulnier; S Claridge

doi:10.1016/s0960-894x(98)00377-1

Probing the importance of spacial and conformational domains in captopril analogs for angiotensin converting enzyme activity

Bioorg Med Chem Lett. 1998 Aug 18;8(16):2123-8. doi: 10.1016/s0960-894x(98)00377-1.

Authors

S Hanessian¹, U Reinhold, M Saulnier, S Claridge

Affiliation

¹ Department of Chemistry, Université de Montréal, Québec, Canada.

PMID: 9873498
DOI: 10.1016/s0960-894x(98)00377-1

Abstract

A new synthesis of 4,5-methano-L-prolines and the enzymatic activity of the corresponding N-(3-mercapto-2-R-methyl-propionyl) analogs as inhibitors of angiotensin converting enzyme are described.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Angiotensin-Converting Enzyme Inhibitors / chemistry*
Angiotensin-Converting Enzyme Inhibitors / pharmacology
Animals
Captopril / analogs & derivatives*
Captopril / chemistry
Captopril / pharmacology
Drug Design
Indicators and Reagents
Isomerism
Lung / enzymology
Models, Molecular
Molecular Conformation
Peptidyl-Dipeptidase A / isolation & purification
Peptidyl-Dipeptidase A / metabolism
Proline / analogs & derivatives*
Proline / chemical synthesis*
Proline / chemistry
Proline / pharmacology
Rabbits
Ramipril / analogs & derivatives
Ramipril / chemistry
Ramipril / pharmacology
Structure-Activity Relationship

Substances

Angiotensin-Converting Enzyme Inhibitors
Indicators and Reagents
ramiprilat
Proline
Captopril
Peptidyl-Dipeptidase A
Ramipril