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  Inhibition of human immunodeficiency virus type 1 reverse transcriptase dimerization using synthetic peptides derived from the connection domain

Divita, G., Restle, T., Goody, R. S., Chermann, J. C., & Baillon, J. G. (1994). Inhibition of human immunodeficiency virus type 1 reverse transcriptase dimerization using synthetic peptides derived from the connection domain. The Journal of Biological Chemistry, 269(18), 13080-13083. Retrieved from http://www.ncbi.nlm.nih.gov/pubmed/7513698.

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JBiolChem_269_1994_13080.pdf (beliebiger Volltext), 522KB
 
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 Urheber:
Divita, Gilles1, Autor           
Restle, Tobias1, 2, Autor           
Goody, Roger S.1, Autor           
Chermann, J. C., Autor
Baillon, J. G., Autor
Affiliations:
1Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society, ou_1497712              
2Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society, ou_1497700              

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 Zusammenfassung: Based on presently available information on the structure of human immunodeficiency virus type 1 (HIV-1) reverse transcriptase, peptides have been synthesized which correspond to the sequence of a particular region of the protein involved in formation of the active heterodimeric form of the enzyme. Several peptides that are 15-19 amino acids long and that are derived from the so-called connection domain of the reverse transcriptase are able to inhibit dimerization of the enzyme and thus inhibit development of its enzymatic activities. In particular, a tryptophan-rich 19-mer corresponding to residues 389-407 was relatively efficient, showing an apparent dissociation constant in the micromolar range for one or both of the subunits. The sequence of this region is identical for both subunits, since one (molecular mass of 51 kDa) is the proteolytic product of the other (molecular mass of 66 kDa). Dissociation of the preformed heterodimer could not be induced by the peptides, but increasing concentrations reduced the rate of dimerization in a concentration-dependent manner until it became immeasurable at high concentrations. The results suggest that inhibition of dimerization of reverse transcriptase is an attractive approach to chemotherapeutic intervention in HIV infection and that further development of peptide-based inhibition strategies is worth pursuing.

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Sprache(n): eng - English
 Datum: 1994-03-101994-05-06
 Publikationsstatus: Erschienen
 Seiten: 4
 Ort, Verlag, Ausgabe: -
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 Art der Begutachtung: Expertenbegutachtung
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Titel: The Journal of Biological Chemistry
  Andere : JBC
Genre der Quelle: Zeitschrift
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Ort, Verlag, Ausgabe: Baltimore, etc. : American Society for Biochemistry and Molecular Biology [etc.]
Seiten: - Band / Heft: 269 (18) Artikelnummer: - Start- / Endseite: 13080 - 13083 Identifikator: ISSN: 0021-9258
CoNE: https://pure.mpg.de/cone/journals/resource/954925410826_1