Characterization of two structurally novel HIV-1 protease inhibitors identified by rational selection
| Autor: | Tammy Antonucci, R. Wong, Robert W. Buckheit, C.C. Humblet, C. Doggett, E.A. Lunney |
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| Rok vydání: | 1993 |
| Předmět: |
T-Lymphocytes
medicine.medical_treatment Molecular Sequence Data Peptide Virus Structure-Activity Relationship HIV Protease HIV-1 protease Virology medicine Retroviral aspartyl protease Humans Amino Acid Sequence Cells Cultured Pharmacology chemistry.chemical_classification Acquired Immunodeficiency Syndrome Protease biology Biological activity Dipeptides HIV Protease Inhibitors Precipitin Tests Kinetics Enzyme Biochemistry chemistry Enzyme inhibitor biology.protein |
| Zdroj: | Antiviral Research. 21:73-84 |
| ISSN: | 0166-3542 |
| Popis: | The human immunodeficiency virus (HIV-1), associated with the AIDS (acquired immunodeficiency syndrome) epidemic, encodes an aspartyl protease that is essential for polyprotein processing in the virus (Navia et al., 1989). It has been demonstrated that inactivation of the protease either catalytically or by an inhibitor prevents infectious virion formation (Kohl et al., 1988; Darke et al., 1989). The acquired knowledge of key molecular interactions occurring between inhibitors and aspartyl proteases, as well as the structural similarities between HIV-1 protease and human renin was used to rationally select candidates for HIV-1 screening from the pool of analogs designed as renin inhibitors. A minimal number of chosen compounds were tested in an HIV-1 protease assay system. Two structurally novel peptides emerged as potent enzymatic protease inhibitors. This study highlights the selection process and characterizes the antiviral properties of the two novel analogs. |
| Databáze: | OpenAIRE |
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