5 results on '"Chakraborty, Chiranjib"'
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2. Insight into Evolution and Conservation Patterns of B1-Subfamily Members of GPCR.
- Author
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Chakraborty, Chiranjib, Sharma, Ashish Ranjan, Sharma, Garima, Bhattacharya, Manojit, and Lee, Sang-Soo
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MEMBRANE proteins , *CYCLIC adenylic acid , *MOLECULAR phylogeny , *SEQUENCE alignment , *PROTEIN receptors - Abstract
The diverse, evolutionary architectures of proteins can be regarded as molecular fossils, tracing a historical path that marks important milestones across life. The B1-subfamily of GPCRs (G-protein-coupled receptors) are medically significant proteins that comprise 15 transmembrane receptor proteins in Homo sapiens. These proteins control the intracellular concentration of cyclic AMP as well as various vital processes in the body. However, little is known about the evolutionary correlation and conservational blueprint of this GPCR subfamily. We performed a comprehensive analysis to understand the evolutionary architecture among 13 members of the B1-subfamily. Multiple sequence alignment analysis exhibited six multiple sequence aligned blocks and five highly aligned blocks. Molecular phylogenetics indicated that CRHR1 and CRHR2 share a typical ancestral relationship and are siblings in 100% bootstrap replications with a total of 24 nodes observed in the cladogram. CRHR2 has the maximum number of extremely conserved amino acids followed by ADCYAP1R1. The longest continuous number sequence logos (74) were found between sequence location 349 and 423, and consequently, the maximum and minimum logo height recorded was 3.6 bits and 0.18 bits, respectively. Finally, to understand the model and pattern of evolutionary relatedness, the conservation blueprint, and the diversification among the members of a protein family, GPCR distribution from several species throughout the animal kingdom was analysed. Together, the study provides an evolutionary insight and offers a rapid method to explore the potential of depicting the evolutionary relationship, conservation blueprint, and diversification among the B1-subfamily of GPCRs using bioinformatics, algorithm analysis, and mathematical models. [ABSTRACT FROM AUTHOR]
- Published
- 2020
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3. Comparative Analysis and Molecular Evolution of Class I PI3K Regulatory Subunit p85α Reveal the Structural Similarity Between nSH2 and cSH2 Domains.
- Author
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Chakraborty, Chiranjib, Sharma, Ashish Ranjan, Sharma, Garima, and Lee, Sang-Soo
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MOLECULAR evolution , *PHOSPHATIDYLINOSITOL 3-kinases , *INSULIN , *POST-translational modification , *PROTEIN structure , *PROTEIN folding - Abstract
Phosphoinositide 3-kinase (PI3K) is an essential regulatory protein of the insulin signaling pathway and several other pathways that govern cell survival, cell proliferation, cell differentiation and oncogene regulation. The protein has main two subunits; regulatory p85 and catalytic p110. Other regulatory subunits are p50, p55. The catalytic activity of p110 is stabilized by the regulatory subunit p85α. This regulatory subunit is composed of five domains; the SH3, BCR-homology (BH), N-terminal SH2 (nSH2), C-terminal SH2 (cSH2), and inter-SH2 (iSH2). In the current study, we executed comparative analysis of the computational proteomic and molecular evolution of these five domains. Our results reveal that faster and more cost-effective methods for forming intricate relationships between the domains are worth pursuing according to vital proteomic parameters such as physico-chemical properties, evolution and post-translational modification (PTM). The results show variation instability, grand average of hydrophobicity (GRAVY), aliphatic index, globularity, PTM among the five domains, and strongly indicate a likeness between the nSH2 and cSH2 domains. The study provides vital information for the structural and functional aspects of PI3K regulatory subunit p85α. Many of these property changes might be defined as protein–protein interactions, protein folding structures and structure–function correlations in future. [ABSTRACT FROM AUTHOR]
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- 2020
- Full Text
- View/download PDF
4. Evaluation and Designing of Epitopic-Peptide Vaccine Against Bunyamwera orthobunyavirus Using M-Polyprotein Target Sequences.
- Author
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Ghosh, Pratik, Bhattacharya, Manojit, Patra, Prasanta, Sharma, Garima, Patra, Bidhan Chandra, Lee, Sang-Soo, Sharma, Ashish Ranjan, and Chakraborty, Chiranjib
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RIFT Valley fever , *VACCINES , *NUCLEAR energy , *PROTEIN-protein interactions , *DYNAMIC simulation , *VACCINE effectiveness , *EPITOPES , *T cells - Abstract
Bunyamwera orthobunyavirus and its serogroup can cause several diseases in humans, cattle, ruminants, and birds. The viral M-polyprotein helps the virus to enter the host body. Therefore, this protein might serve as a potential vaccine target against Bunyamwera orthobunyavirus. The present study applied the immunoinformatics technique to design an epitopic vaccine component that could protect against Bunyamwera infection. Phylogenetic analysis revealed the presence of conserved patterns of M-polyprotein within the viral serogroup. Three epitopes common for both B-cell and T-cell were identified, i.e., YQPTELTRS, YKAHDKEET, and ILGTGTPKF merged with a specific linker peptide to construct an active vaccine component. The low atomic contact energy value of docking complex between human TLR4 (TLR4/MD2 complex) and vaccine construct confirms the elevated protein–protein binding interaction. Molecular dynamic simulation and normal mode analysis illustrate the docking complex's stability, especially by the higher Eigenvalue. In silico cloning of the vaccine construct was applied to amplify the desired vaccine component. Structural allocation of both the vaccine and epitopes also show the efficacy of the developed vaccine. Hence, the computational research design outcomes support that the peptide-based vaccine construction is a crucial drive target to limit the infection of Bunyamwera orthobunyavirus to an extent. [ABSTRACT FROM AUTHOR]
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- 2022
- Full Text
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5. A Novel Multi-Epitopic Peptide Vaccine Candidate Against Helicobacter pylori: In-Silico Identification, Design, Cloning and Validation Through Molecular Dynamics.
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Ghosh, Pratik, Bhakta, Swarnav, Bhattacharya, Manojit, Sharma, Ashish Ranjan, Sharma, Garima, Lee, Sang-Soo, and Chakraborty, Chiranjib
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HELICOBACTER pylori , *MOLECULAR dynamics , *RIBOSOMAL proteins , *VACCINES , *MOLECULAR cloning , *MOLECULAR docking , *CLARITHROMYCIN , *CD19 antigen - Abstract
Helicobacter pylori is a highly potential pathogen to colonize in the human stomach. This bacterial strain is now alarming serious health concern all over the world. Combating through available drugs is a difficult task due to lack of appropriate common targets against genetically diverse strains. Therefore, the developments of effective targets vaccines require alternative strategies to eliminate the H. pylori infection. In this study, we developed a novel vaccine construct using B-cell derived T-cell epitopes from four target antigenic proteins (HpaA, FlaA, FlaB and Omp18), and found the induction of possible immune response using advanced immunoinformatics approaches. In order to boost immune system, we tagged adjuvant (50S ribosomal protein L7/L12) with a suitable linker at the N-terminus side of vaccine sequence. Protein–protein docking between human Toll like receptor 5 (TLR5) and vaccine construct help to predict the way of inductive signaling that leads to immune-response. The calculated negative score (− 151.4, + / − 8.7) of molecular docking complex signify the best binding interface. Molecular dynamics simulation studies confirmed the proper docking between TLR5 and vaccine candidate. Moreover, Normal mode analysis (NMA) calculates the molecular motion of the docking complex. The low eigenvalue (2.935e−05) indicates the stable and flexible molecular motion in the binding interaction side. Finally, in-silico cloning of vaccine candidate was performed using expression vector pET28b (+) with the optimized restriction sites. [ABSTRACT FROM AUTHOR]
- Published
- 2021
- Full Text
- View/download PDF
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