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Virtual Screening and Prediction of Binding of Caprine CSN1S2 Protein Tryptic Peptides to Glucokinase.

ABSTRACT: Introduction:Glucokinase (hexokinase D) is an enzyme that phosphorylates glucose in hepatocytes totrap it in the cell and prime it for conversion to other compounds, yet this enzyme has low affinity to bind with glucose. In Diabetes Mellituspatients, the blood glucose level is poorly controled. Material and Methods:This study explored the possibility to induce glucokinase activity with bioactive peptides derived from the goat milk protein CSN1S2 by in- silico docking approach. Two bioactive tryptic peptides, CSN1S2 residues 41-47 and 214-221, were successfully docked to glucokinase and found to bind to the activation site. Results:Amino acid residues Asn41, Ala43, His45 and Arg221 from these peptides provided the major contribution to docking to glucokinase. Asn41 made more interactions with glucokinase than the other residues in the peptide, including hydrogen bonds and salt-bridge These bioactive peptides appear to help glucokinase to bind glucose, since the number of hydrogen bonds between the protein and the glucose was higher and their distances shorter in the complex with the peptides without disturbing the glucose position for phosphorylation. Conclusion:Thus, the activation effect of the CSN1S2 derived bioactive peptides for glucokinase binding affinity of glucose is indicated by this study.

SUBMITTER: Fatchiyah F

PROVIDER: S-EPMC5723197 | biostudies-literature | 2017 Dec

REPOSITORIES: biostudies-literature

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Virtual Screening and Prediction of Binding of Caprine CSN1S2 Protein Tryptic Peptides to Glucokinase.

Fatchiyah Fatchiyah F Rahasta Atika Hanoum AH Cairns James R Ketudat JRK

Acta informatica medica : AIM : journal of the Society for Medical Informatics of Bosnia & Herzegovina : casopis Drustva za medicinsku informatiku BiH 20171201 4

<h4>Introduction</h4>Glucokinase (hexokinase D) is an enzyme that phosphorylates glucose in hepatocytes totrap it in the cell and prime it for conversion to other compounds, yet this enzyme has low affinity to bind with glucose. In Diabetes Mellituspatients, the blood glucose level is poorly controled.<h4>Material and methods</h4>This study explored the possibility to induce glucokinase activity with bioactive peptides derived from the goat milk protein CSN1S2 by in- silico docking approach. Two ...[more]

PMID: 29284910

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Project description:Hepatitis E virus (HEV) is the notable causative agent of acute and chronic hepatic, renal, pancreatic, neurological, and hematopoietic blood cell infections with high risk in immunocompromised patients. Hepatic failure is mostly documented among adults, pregnant women, and patients with preexisting liver disease. HEV is a positive sense RNA virus of 7.2 kb genome size with typically three open reading frames (ORFs) which play essential roles in viral replication, genome assembly, and transcription. The mutational substitution in the viral RNA genome makes more it difficult to understand the actual relationship in the host-virus association. ORFs of HEV encode different structural and non-structural proteins and one of them is the capsid protein which is coded by ORF2. The capsid protein mediates the encapsulation of the viral genome as well as being involved in virion assembly. In the current study, the ligand-based docking approach was employed to inhibit the active amino acids of the viral capsid protein. Depending upon S-score, ADMET profiling, and drug scanning, the top ten tetrapeptides were selected as potential drug candidates with no toxicity counter to HEV receptor protein. The S-score or docking score is a mathematical function which predicts the binding affinities of docked complexes. The binding affinity of the predicted drug-target complexes helps in the selectivity of the desired compound as a potential drug. The best two selected peptides (i.e., TDGH with S-score of -8.5 and EGDE with S-score of -8.0) interacted with the active site amino acids of the capsid protein (i.e., Arg399, Gln420, and Asp444). The molecular dynamics simulations of RMSD trajectories of TDGH-capsid protein and EDGE-capsid protein have revealed that both docked complexes were structurally stable. The study revealed that these tetrapeptides would serve as strong potential inhibitors and a starting point for the development of new drug molecules against the HEV capsid protein. In future, in vivo studies are needed to explore selected peptides as potential drug candidates.

Dataset Information

Virtual Screening and Prediction of Binding of Caprine CSN1S2 Protein Tryptic Peptides to Glucokinase.

Publications

Virtual Screening and Prediction of Binding of Caprine CSN1S2 Protein Tryptic Peptides to Glucokinase.

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