tailieunhanh - Báo cáo khoa học: Peptides that bind the HIV-1 integrase and modulate its enzymatic activity – kinetic studies and mode of action

Several peptides that specifically bind the HIV-1 integrase (IN) and either inhibit or stimulate its enzymatic activity were developed in our laborato-ries. Kinetic studies using 3¢-end processing and strand-transfer assays were performed to study the mode of action of these peptides. | BFEBS Journal Peptides that bind the HIV-1 integrase and modulate its enzymatic activity - kinetic studies and mode of action Aviad Levin1 Hadar Benyamini2 Zvi Hayouka2 Assaf Friedler2 and Abraham Loyter1 1 Department of BiologicalChemistry The Alexander Silberman Institute of Life Sciences The Hebrew University of Jerusalem Israel 2 Institute of Chemistry The Alexander Silberman Institute of Life Sciences The Hebrew University of Jerusalem Israel Keywords HIV-1 integrase peptides Correspondence A. Loyter Department of Biological Chemistry The Alexander Silberman Institute of Life Sciences The Hebrew University of Jerusalem Safra Campus Givat Ram Jerusalem 91904 Israel Fax 972 2 658 6448 Tel 972 2 658 5422 E-mail loyter@ Received 21 April 2010 revised 1 November 2010 accepted 5 November 2010 doi Several peptides that specifically bind the HIV-1 integrase IN and either inhibit or stimulate its enzymatic activity were developed in our laboratories. Kinetic studies using 3 -end processing and strand-transfer assays were performed to study the mode of action of these peptides. The effects of the various peptides on the interaction between IN and its substrate DNA were also studied by fluorescence anisotropy. On the basis of our results we divided these IN-interacting peptides into three groups a IN-inhibitory peptides whose binding to IN decrease its affinity for the substrate DNA - these peptides increased the Km of the IN-DNA interaction and were thus inhibitory b peptides that slightly increased the Km of the IN-DNA interaction but in addition modified the Vmax and Kcat values of the IN and thus stimulated or inhibited IN activity respectively and c peptides that bound IN but had no effect on its enzymatic activity. We elucidated the approximate binding sites of the peptides in the structure of IN providing structural insights into their mechanism of action. The IN-stimulating peptide bound IN in several specific sites .

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