Inhibition of HIV-1 protease by short peptides derived from the terminal segments of the protease
The active HIV-1 protease is a homodimeric enzyme. A β-sheet consisting of N- and C-terminal segments provides the main driving force for dimerization of the inactive protomers. Several short peptides with sequences derived from the N- and C-termini of the protease were tested for inhibition of prot...
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| Veröffentlicht in: | Biochemical and biophysical research communications 1992-04, Vol.184 (2), p.980-985 |
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| container_title | Biochemical and biophysical research communications |
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| creator | Schramm, Hans J. Breipohl, Gerhard Hansen, Jutta Henke, Stephan Jaeger, Ernst Meichsner, Christoph Rieß, Günther Ruppert, Dieter Rücknagel, Karl-Peter Schäfer, Wolfram Schramm, Wolfgang |
| description | The active HIV-1 protease is a homodimeric enzyme. A β-sheet consisting of N- and C-terminal segments provides the main driving force for dimerization of the inactive protomers. Several short peptides with sequences derived from the N- and C-termini of the protease were tested for inhibition of protease activity and for inhibition of HIV-1 replication in lymphocytes. Medium inhibitory activity was found with each of the peptides in the enzyme test and no inhibition of the lymphocytes was found up to 200 μg/ml. The enzyme tests indicate that HIV-1 protease is the target of the inhibitory action. Synergistic action could not be found with pairs of the peptides derived from the two different termini. Prolonged incubation with one of the peptides increased inhibition indicating a slow dissociation of the protease dimers. No cytotoxic effect of the inhibitors could be found below 200 μg/ml. |
| doi_str_mv | 10.1016/0006-291X(92)90687-G |
| format | Article |
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A β-sheet consisting of N- and C-terminal segments provides the main driving force for dimerization of the inactive protomers. Several short peptides with sequences derived from the N- and C-termini of the protease were tested for inhibition of protease activity and for inhibition of HIV-1 replication in lymphocytes. Medium inhibitory activity was found with each of the peptides in the enzyme test and no inhibition of the lymphocytes was found up to 200 μg/ml. The enzyme tests indicate that HIV-1 protease is the target of the inhibitory action. Synergistic action could not be found with pairs of the peptides derived from the two different termini. Prolonged incubation with one of the peptides increased inhibition indicating a slow dissociation of the protease dimers. No cytotoxic effect of the inhibitors could be found below 200 μg/ml.</description><identifier>ISSN: 0006-291X</identifier><identifier>EISSN: 1090-2104</identifier><identifier>DOI: 10.1016/0006-291X(92)90687-G</identifier><identifier>PMID: 1575762</identifier><identifier>CODEN: BBRCA9</identifier><language>eng</language><publisher>San Diego, CA: Elsevier Inc</publisher><subject>AIDS/HIV ; Amino Acid Sequence ; Antibiotics. Antiinfectious agents. Antiparasitic agents ; Antiviral agents ; Antiviral Agents - chemical synthesis ; Antiviral Agents - pharmacology ; Biological and medical sciences ; C-terminus ; Cells, Cultured ; HIV Protease - genetics ; HIV Protease Inhibitors ; HIV-1 - enzymology ; HIV-1 - physiology ; human immunodeficiency virus 1 ; Humans ; inhibition ; Interleukin-2 - pharmacology ; Kinetics ; Lymphocytes ; Medical sciences ; Molecular Sequence Data ; N-terminus ; Oligopeptides - pharmacology ; peptides ; Pharmacology. 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A β-sheet consisting of N- and C-terminal segments provides the main driving force for dimerization of the inactive protomers. Several short peptides with sequences derived from the N- and C-termini of the protease were tested for inhibition of protease activity and for inhibition of HIV-1 replication in lymphocytes. Medium inhibitory activity was found with each of the peptides in the enzyme test and no inhibition of the lymphocytes was found up to 200 μg/ml. The enzyme tests indicate that HIV-1 protease is the target of the inhibitory action. Synergistic action could not be found with pairs of the peptides derived from the two different termini. Prolonged incubation with one of the peptides increased inhibition indicating a slow dissociation of the protease dimers. No cytotoxic effect of the inhibitors could be found below 200 μg/ml.</description><subject>AIDS/HIV</subject><subject>Amino Acid Sequence</subject><subject>Antibiotics. Antiinfectious agents. Antiparasitic agents</subject><subject>Antiviral agents</subject><subject>Antiviral Agents - chemical synthesis</subject><subject>Antiviral Agents - pharmacology</subject><subject>Biological and medical sciences</subject><subject>C-terminus</subject><subject>Cells, Cultured</subject><subject>HIV Protease - genetics</subject><subject>HIV Protease Inhibitors</subject><subject>HIV-1 - enzymology</subject><subject>HIV-1 - physiology</subject><subject>human immunodeficiency virus 1</subject><subject>Humans</subject><subject>inhibition</subject><subject>Interleukin-2 - pharmacology</subject><subject>Kinetics</subject><subject>Lymphocytes</subject><subject>Medical sciences</subject><subject>Molecular Sequence Data</subject><subject>N-terminus</subject><subject>Oligopeptides - pharmacology</subject><subject>peptides</subject><subject>Pharmacology. Drug treatments</subject><subject>proteinase</subject><subject>Recombinant Proteins - pharmacology</subject><subject>Structure-Activity Relationship</subject><subject>Virus Replication - drug effects</subject><issn>0006-291X</issn><issn>1090-2104</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1992</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkU9vFDEMxSMEKtvCNwApB4TKYcDOTJLNpRKqYLtSJS6AuEWZxMMGzZ8lyVbqt2eGXcoNTj68n5_tZ8ZeILxFQPUOAFQlDH67NOKNAbXW1eYRWyEYqARC85itHpCn7DznHwCIjTJn7AylllqJFXPbcRfbWOI08qnjN9uvFfJ9mgq5TLy953k3pcL3tC8xUOaBUryjwLs0DbzsiBdKQxxdzzN9H2gsebFZhD8mz9iTzvWZnp_qBfvy8cPn65vq9tNme_3-tvIN6lKFtjaESpuW1tKFMC_aeOWga0ECgtc1dDIY35GvoYWuBhTYzAd5WGuJur5gr4--8-CfB8rFDjF76ns30nTIVs85rBtZ_xdEJWoFKGewOYI-TTkn6uw-xcGle4tglxfYJV-75GuNsL9fYDdz28uT_6EdKPxtOmY-669Ousve9V1yo4_5AZPCKKHVjF0dMZpDu4uUbPaRRk8hJvLFhin-e49feWeh_A</recordid><startdate>19920430</startdate><enddate>19920430</enddate><creator>Schramm, Hans J.</creator><creator>Breipohl, Gerhard</creator><creator>Hansen, Jutta</creator><creator>Henke, Stephan</creator><creator>Jaeger, Ernst</creator><creator>Meichsner, Christoph</creator><creator>Rieß, Günther</creator><creator>Ruppert, Dieter</creator><creator>Rücknagel, Karl-Peter</creator><creator>Schäfer, Wolfram</creator><creator>Schramm, Wolfgang</creator><general>Elsevier Inc</general><general>Elsevier</general><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QL</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>M81</scope><scope>P64</scope><scope>7X8</scope></search><sort><creationdate>19920430</creationdate><title>Inhibition of HIV-1 protease by short peptides derived from the terminal segments of the protease</title><author>Schramm, Hans J. ; Breipohl, Gerhard ; Hansen, Jutta ; Henke, Stephan ; Jaeger, Ernst ; Meichsner, Christoph ; Rieß, Günther ; Ruppert, Dieter ; Rücknagel, Karl-Peter ; Schäfer, Wolfram ; Schramm, Wolfgang</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c417t-db39e1679be85add1464c6a0fb05010c730f5d9cfec30b0f301214011c0875173</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1992</creationdate><topic>AIDS/HIV</topic><topic>Amino Acid Sequence</topic><topic>Antibiotics. 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A β-sheet consisting of N- and C-terminal segments provides the main driving force for dimerization of the inactive protomers. Several short peptides with sequences derived from the N- and C-termini of the protease were tested for inhibition of protease activity and for inhibition of HIV-1 replication in lymphocytes. Medium inhibitory activity was found with each of the peptides in the enzyme test and no inhibition of the lymphocytes was found up to 200 μg/ml. The enzyme tests indicate that HIV-1 protease is the target of the inhibitory action. Synergistic action could not be found with pairs of the peptides derived from the two different termini. Prolonged incubation with one of the peptides increased inhibition indicating a slow dissociation of the protease dimers. No cytotoxic effect of the inhibitors could be found below 200 μg/ml.</abstract><cop>San Diego, CA</cop><pub>Elsevier Inc</pub><pmid>1575762</pmid><doi>10.1016/0006-291X(92)90687-G</doi><tpages>6</tpages></addata></record> |
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| ispartof | Biochemical and biophysical research communications, 1992-04, Vol.184 (2), p.980-985 |
| issn | 0006-291X 1090-2104 |
| language | eng |
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| source | MEDLINE; Elsevier ScienceDirect Journals |
| subjects | AIDS/HIV Amino Acid Sequence Antibiotics. Antiinfectious agents. Antiparasitic agents Antiviral agents Antiviral Agents - chemical synthesis Antiviral Agents - pharmacology Biological and medical sciences C-terminus Cells, Cultured HIV Protease - genetics HIV Protease Inhibitors HIV-1 - enzymology HIV-1 - physiology human immunodeficiency virus 1 Humans inhibition Interleukin-2 - pharmacology Kinetics Lymphocytes Medical sciences Molecular Sequence Data N-terminus Oligopeptides - pharmacology peptides Pharmacology. Drug treatments proteinase Recombinant Proteins - pharmacology Structure-Activity Relationship Virus Replication - drug effects |
| title | Inhibition of HIV-1 protease by short peptides derived from the terminal segments of the protease |
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