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Molecular Characterization and Drug Designing against Hypothetical Proteins of Aspergillus fumigatus Af293 by Homology Modeling and Molecular Docking


Affiliations
1 Department of Genetic Engineering and Biotechnology, University of Chittagong, Chittagong - 4331, Bangladesh
2 Department of Biochemistry and Biotechnology, University of Science and Technology, Chittagong, Bangladesh
3 Department of Computer Science and Engineering, Atish Dipankar University of Science and Technology, Dhaka - 1213, Bangladesh
4 Department of Biochemistry and Biotechnology, University of Science and Technology, Chittagong, India
     

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Genome sequencing projects have led to an explosion of the huge amount of gene products in which many are of Hypothetical Proteins (HPs) with an unidentified function. Exploring and annotating the functions of HPs is important in (Aspergillus fumigatus) which is a pathogenic fungus that cause disease in individuals associated with immunodeficiency. In this study, sequence of five HPs of (A. fumigatus Af293), which are nonhomologous to human, has been annotated from NCBI. Various computational tools such as three-dimensional (3D) structure was determined by means of homology modeling through Phyre2 and refined by ModRefiner. Then, the designed structure was evaluated with a structure validation program for instance ERRAT, PROCHECK, and QMEAN, for further structural analysis. The secondary structural features of proteins were determined through self-optimized prediction method with alignment and interacting networks by STRING. The receptor was analyzed by the active site and pocket finder tools. Docking studies were done through AutodockVina software. The 3D structure of five proteins was modeled and their ligand binding sites were identified. We have found domains and families of two proteins and these revealed that these proteins might have adenosine diphosphate-ribosylation activity, molecular chaperone, heat shock protein activity, plasminogen/hepatocyte growth factor activity, etc. Protein-ligand study of our predicted ligand shows the lowest energy of -7.4 kcal/mol for gi|66851587 and -6.7 kcal/mol for gi|66845370. Structural prediction of these proteins, detection of binding sites, and drug designing of current study will cover the way for further extensive investigation of these proteins in wet laboratory experiments and in that way assist drug design against Aspergillosis.

Keywords

Aspergillosis, (Aspergillus fumigatus Af293), Docking Analysis, Homology Modeling, Hypothetical Protein.
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  • Molecular Characterization and Drug Designing against Hypothetical Proteins of Aspergillus fumigatus Af293 by Homology Modeling and Molecular Docking

Abstract Views: 520  |  PDF Views: 0

Authors

Shah Md. Shahik
Department of Genetic Engineering and Biotechnology, University of Chittagong, Chittagong - 4331, Bangladesh
Towhidur Rahman
Department of Biochemistry and Biotechnology, University of Science and Technology, Chittagong, Bangladesh
Srabasti Ghosh
Department of Biochemistry and Biotechnology, University of Science and Technology, Chittagong, Bangladesh
Ismot Ara
Department of Computer Science and Engineering, Atish Dipankar University of Science and Technology, Dhaka - 1213, Bangladesh
Sabrina Amin
Department of Biochemistry and Biotechnology, University of Science and Technology, Chittagong, India
Md. Amzad Hossain
Department of Genetic Engineering and Biotechnology, University of Chittagong, Chittagong - 4331, Bangladesh
Yeasmeen Ali
Department of Genetic Engineering and Biotechnology, University of Chittagong, Chittagong - 4331, Bangladesh
Abdul Musaweer Habib
Department of Genetic Engineering and Biotechnology, University of Chittagong, Chittagong - 4331, Bangladesh
Mohd. Omar Faruk Sikder
Department of Genetic Engineering and Biotechnology, University of Chittagong, Chittagong - 4331, Bangladesh

Abstract


Genome sequencing projects have led to an explosion of the huge amount of gene products in which many are of Hypothetical Proteins (HPs) with an unidentified function. Exploring and annotating the functions of HPs is important in (Aspergillus fumigatus) which is a pathogenic fungus that cause disease in individuals associated with immunodeficiency. In this study, sequence of five HPs of (A. fumigatus Af293), which are nonhomologous to human, has been annotated from NCBI. Various computational tools such as three-dimensional (3D) structure was determined by means of homology modeling through Phyre2 and refined by ModRefiner. Then, the designed structure was evaluated with a structure validation program for instance ERRAT, PROCHECK, and QMEAN, for further structural analysis. The secondary structural features of proteins were determined through self-optimized prediction method with alignment and interacting networks by STRING. The receptor was analyzed by the active site and pocket finder tools. Docking studies were done through AutodockVina software. The 3D structure of five proteins was modeled and their ligand binding sites were identified. We have found domains and families of two proteins and these revealed that these proteins might have adenosine diphosphate-ribosylation activity, molecular chaperone, heat shock protein activity, plasminogen/hepatocyte growth factor activity, etc. Protein-ligand study of our predicted ligand shows the lowest energy of -7.4 kcal/mol for gi|66851587 and -6.7 kcal/mol for gi|66845370. Structural prediction of these proteins, detection of binding sites, and drug designing of current study will cover the way for further extensive investigation of these proteins in wet laboratory experiments and in that way assist drug design against Aspergillosis.

Keywords


Aspergillosis, (Aspergillus fumigatus Af293), Docking Analysis, Homology Modeling, Hypothetical Protein.

References





DOI: https://doi.org/10.22506/ti%2F2015%2Fv22%2Fi3%2F137626