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Title: | Occupation of a thermoresistant-scaffold (αRep) at SP1-NC cleavage site disturbs the function of HIV-1 protease |
Authors: | Sudarat Hadpech Nichakan Peerakam Koollawat Chupradit Chatchai Tayapiwatana |
Authors: | Sudarat Hadpech Nichakan Peerakam Koollawat Chupradit Chatchai Tayapiwatana |
Keywords: | Biochemistry, Genetics and Molecular Biology |
Issue Date: | 1-Jun-2020 |
Abstract: | © 2020 Portland Press Ltd. All rights reserved. HIV-1 nucleocapsid (NC) becomes an attractive target for the development of novel anti-HIV-1 agents. Discovering of non-antibody scaffolds that disrupt the function of NC will be a potential aspect for disturbing viral maturation process. Correspondingly, we explored the specific binding site of the thermoresistant-scaffold protein, αRep9A8 which formerly demonstrated the inhibitory effect on HIV-1 replication. The portion of Gag, CA21-SP1-NC has been used as a template for designing nine overlapping peptides (P4-P12). The P9 peptide showed the strongest binding activity followed by P8 and P12 respectively. The amino acid sequences on those peptides resemble the N-terminal domain of the NC proximity to the SP1-NC initial cleavage site and across the conserved CCHC zinc finger 1 (ZF1) of NC. The interaction KD between αRep9A8 with its target was 224.9 +− 57.4 nM. Consequently, αRep9A8 demonstrated the interference of the HIV-1 protease function by hindering a protease cleavage site. The released NC product from CA21-SP1-NC was diminished. The present study provided an additional information of αRep9A8 function in interfering of viral maturation processes resulting in the decremental efficiency of viral infectivity. |
URI: | https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=85087096640&origin=inward http://cmuir.cmu.ac.th/jspui/handle/6653943832/70227 |
ISSN: | 15734935 01448463 |
Appears in Collections: | CMUL: Journal Articles |
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