An unusual functional group interaction and its potential to reproduce steric and electrostatic features of the transition states of peptidolysis

Bioorganic and Medicinal Chemistry

Volumn 14, Issue 11, 2006, Pages 3835-3847

  Gautier, Arnaud ^a   Pitrat, Delphine ^a   Hasserodt, Jens ^a  

^a UNIVERSITÉ DE LYON   (France)

Author keywords

Aspartic peptidases; Asymmetric synthesis; Conformational analysis; Enzyme inhibitors; Nucleophile electrophile interactions; Peptidomimetics

Indexed keywords

ENZYME INHIBITOR; METHANOL; PEPTIDASE; PEPTIDASE INHIBITOR; UNCLASSIFIED DRUG; WATER;

ARTICLE; CHEMICAL INTERACTION; CONFORMATIONAL TRANSITION; DRUG CONFORMATION; DRUG DESIGN; DRUG STRUCTURE; DRUG SYNTHESIS; ENZYME ACTIVITY; ENZYME INHIBITION; FLUORESCENCE RESONANCE ENERGY TRANSFER; HUMAN IMMUNODEFICIENCY VIRUS 1; HYDROLYSIS; IC 50; SOLUBILITY; TEMPERATURE SENSITIVITY;

ALDEHYDES; AMINES; ELECTROSTATICS; HIV-1; HYDROGEN BONDING; HYDROLYSIS; KINETICS; MOLECULAR CONFORMATION; PEPTIDE HYDROLASES; PEPTIDES; PROTEIN FOLDING; SOLUBILITY; STEREOISOMERISM; STRUCTURE-ACTIVITY RELATIONSHIP; TEMPERATURE;

HUMAN IMMUNODEFICIENCY VIRUS 1;

EID: 33646071810     PISSN: 09680896     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bmc.2006.01.031     Document Type: Article

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