Thongkum, Weeraya and Samerjai, Kanokwan and Saoin, Somphot and Wisitponchai, Tanchanok and Hadpech, Sudarat and Lee, Vannajan Sanghiran and Lim, Theam Soon and Tayapiwatana, Chatchai (2018) Selection of Ankyrin Targeting HIV-1 Matrix and Identification of Its Binding Domain. Chiang Mai University Journal of Natural Sciences, 17 (4). pp. 339-362. ISSN 1685-1994, DOI https://doi.org/10.12982/CMUJNS.2018.0024.
Full text not available from this repository.Abstract
Ankyrin repeat protein is a novel class of non-antibody binding protein that can be applied as an alternative antiretroviral agent. Engineered ankyrin targeting the HIV-1 matrix (MA) would be a promising agent to interfere with HIV replication, since MA plays a major role in multiple processes of the viral life cycle. In this study, MA-specific ankyrin (AnkGAGG31) was isolated from an artificial ankyrin library using a semi-automated selection process with biotinylated MA-streptavidin magnetic beads. The AnkGAGG31-recognition site on MA was determined using both indirect and competitive ELISAs with overlapping MA tri-helical fragments and pentadecapeptides. The AnkGAGG31 showed the highest binding signal to the MA-fragments covering helices 2-3-4 and peptides corresponding to helix 2 (residues 25-43), which were found as the target epitope. This finding was further analyzed by molecular modeling and docking. The rational models of AnkGAGG31-MA complex indicated that the strong binding interaction was shown on helix 2 at key residues K27MA, K30M, and K32MA. Taken together, the identification of the binding domain on the MA target improves our understanding of the AnkGAGG31-MA interaction and provides the information necessary to design innovative protein targeting of the MA protein.
| Item Type: | Article |
|---|---|
| Funders: | UNSPECIFIED |
| Uncontrolled Keywords: | Ankyrin; Binding domain; HIV-1 matrix; MA protein; Phage-displayed panning |
| Subjects: | Q Science > Q Science (General) Q Science > QD Chemistry |
| Divisions: | Faculty of Science > Department of Chemistry |
| Depositing User: | Ms. Juhaida Abd Rahim |
| Date Deposited: | 25 Feb 2019 03:57 |
| Last Modified: | 25 Feb 2019 03:57 |
| URI: | http://eprints.um.edu.my/id/eprint/20472 |
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