Similarity in the Amino Acid Sequences of Mycobacterium tuberculosis Protein Targets Involved in Binding Sites of Docking with Thiacetazone
| Autor: | Mafakheri M, Sardari S |
|---|---|
| Rok vydání: | 2016 |
| Předmět: |
0301 basic medicine
Drug chemistry.chemical_classification Tuberculosis biology media_common.quotation_subject Computational biology biology.organism_classification Bioinformatics medicine.disease Amino acid Mycobacterium tuberculosis 03 medical and health sciences 030104 developmental biology 0302 clinical medicine chemistry Docking (molecular) medicine 030212 general & internal medicine Binding site Peptide sequence Mycobacterium media_common |
| Zdroj: | Pharmaceutica Analytica Acta. 7 |
| ISSN: | 2153-2435 |
| DOI: | 10.4172/2153-2435.1000509 |
| Popis: | Although according to WHO document, between 1990 and 2015, both TB mortality and its incidence has been fallen over 47% worldwide, the spread of multidrug-resistant strains of Mycobacterium tuberculosis reveals clearly that the efforts to find new drugs should not be stopped and the pathogenic microorganisms develop resistance. More extended knowledge about existing drugs is critical to design new and more effective medicines. In this study, we report the amino acid sequences involved in binding sites of 70 M. tuberculosis protein targets’ docked with Thiacetazone (TAC), one of the extensively used antitubercular drug that is used in combination with other antitubercular agents to break multi-drug resistant TB. Categorization of protein targets was performed on the basis of the free energy of binding for the docked compounds. Comparison of the binding sites with the aim of ClustalW application indicated huge similarities in their amino acid sequences among target complexes. |
| Databáze: | OpenAIRE |
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