Computational approaches in targeting monkeypox virus: a focus on phytochemical inhibition of profilin-like protein A42R (Record no. 23008)

MARC details
000 -LEADER
fixed length control field a
003 - CONTROL NUMBER IDENTIFIER
control field OSt
005 - DATE AND TIME OF LATEST TRANSACTION
control field 20250621094707.0
008 - FIXED-LENGTH DATA ELEMENTS--GENERAL INFORMATION
fixed length control field 250621b xxu||||| |||| 00| 0 eng d
040 ## - CATALOGING SOURCE
Original cataloging agency AIKTC-KRRC
Transcribing agency AIKTC-KRRC
100 ## - MAIN ENTRY--PERSONAL NAME
9 (RLIN) 26520
Author Shorna, Afsana Amin
245 ## - TITLE STATEMENT
Title Computational approaches in targeting monkeypox virus: a focus on phytochemical inhibition of profilin-like protein A42R
250 ## - EDITION STATEMENT
Volume, Issue number Vol.14(4), Oct-Dec
260 ## - PUBLICATION, DISTRIBUTION, ETC.
Place of publication, distribution, etc. Raipur
Name of publisher, distributor, etc. Asian Pharma Press
Year 2024
300 ## - PHYSICAL DESCRIPTION
Pagination 355-362p.
520 ## - SUMMARY, ETC.
Summary, etc. Monkeypox, a viral infection caused by the Monkeypox virus (MPXV), poses a significant public health threat. To identify potential antiviral metabolites against MPXV, we focused on the monkeypox profilin-like protein, crucial for viral replication. Twenty metabolites from various classes were retrieved from PubChem for molecular dynamics simulations. The top three molecules—Melongoside N, CID-4483043, Avenacosid A, CID-267363, and Melongoside P, CID- 131750951 demonstrated the best binding affinity for Profilin-like Protein A42R (PDB-4QWO). These ligands displayed stable interactions and minimal structural fluctuations during simulations, as indicated by favorable RMSD, RMSF, Rg, SASA, MolSA, and PSA results. The ligands maintained acceptable conformational stability with RMSD values within 1–3 Å, showing minimal structural changes. The ligands exhibited stable interactions with specific protein residues, indicating consistent and limited local alterations in the protein structure. Throughout a 250 ns simulation, the ligands maintained the protein's compactness, with average Rg values suggesting no major structural changes. Ligand complexes displayed typical van der Waals surface areas and polar interactions, supporting their stable interaction with the target protein. These ligands show promise as antiviral agents against monkeypox, with in-silico findings providing valuable insights for drug design. However, further experimental validation is crucial to advancing these ligands toward tangible antiviral therapeutics. This study contributes vital information to the computational drug discovery field, emphasizing interdisciplinary approaches for effective viral infection control.<br/>
650 #0 - SUBJECT ADDED ENTRY--TOPICAL TERM
9 (RLIN) 4639
Topical term or geographic name entry element PHARMACEUTICS
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9 (RLIN) 15300
Co-Author Farhana Rahman
773 0# - HOST ITEM ENTRY
International Standard Serial Number 2231-5683
Title Asian journal of pharmaceutical research
Place, publisher, and date of publication Raipur Asian Pharma Press
856 ## - ELECTRONIC LOCATION AND ACCESS
URL https://asianjpr.com/AbstractView.aspx?PID=2024-14-4-2
Link text Click here
942 ## - ADDED ENTRY ELEMENTS (KOHA)
Source of classification or shelving scheme Dewey Decimal Classification
Koha item type Articles Abstract Database
Holdings
Withdrawn status Lost status Source of classification or shelving scheme Damaged status Not for loan Home library Current library Shelving location Date acquired Total Checkouts Barcode Date last seen Price effective from Koha item type
    Dewey Decimal Classification     School of Pharmacy School of Pharmacy Archieval Section 21/06/2025   2025-0967 21/06/2025 21/06/2025 Articles Abstract Database
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