Element '{http://www.crossref.org/schema/4.3.6}journal_volume': This element is not expected. Expected is one of ( {http://www.crossref.org/schema/4.3.6}contributors, {http://www.crossref.org/schema/4.3.6}publication_date ).
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<doi_batch xmlns="http://www.crossref.org/schema/4.3.6" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance" xmlns:jats="http://www.ncbi.nlm.nih.gov/JATS1" xmlns:ai="http://www.crossref.org/AccessIndicators.xsd" version="4.3.6" xsi:schemaLocation="http://www.crossref.org/schema/4.3.6 https://www.crossref.org/schemas/crossref4.3.6.xsd">
<head>
<doi_batch_id>_1765500929</doi_batch_id>
<timestamp>1765500929</timestamp>
<depositor>
<depositor_name>Abasyn University Peshawar</depositor_name>
<email_address>sufi.ali.ahmad@abasyn.edu.pk</email_address>
</depositor>
<registrant>Abasyn University</registrant>
</head>
<body>
<journal>
<journal_metadata>
<full_title>Abasyn Journal of Life Sciences</full_title>
<abbrev_title>AJ Life Sci.</abbrev_title>
<issn media_type="electronic">2663-1040</issn>
<issn media_type="print">2616-9754</issn>
</journal_metadata>
<journal_issue>
<journal_volume>
<volume>7</volume>
</journal_volume>
<issue>7</issue>
</journal_issue>
<journal_article xmlns:jats="http://www.ncbi.nlm.nih.gov/JATS1" xmlns:ai="http://www.crossref.org/AccessIndicators.xsd" publication_type="full_text" metadata_distribution_opts="any">
<titles>
<title>Exploring Novel Alanine Racemase Enzyme Inhibitors Using Cheminformatics and Biophysics Techniques</title>
</titles>
<contributors>
<person_name contributor_role="author" sequence="first">
<given_name>Bilal</given_name>
<surname>Shaker</surname>
</person_name>
</contributors>
<jats:abstract xmlns:jats="http://www.ncbi.nlm.nih.gov/JATS1">
<jats:p>Antibiotic resistance in bacteria is rapidly increasing across the globe which warrants the development of new drugs to tackle this issue. Herein, using clerodane furanolactones as a parent structure, we identified several derivatives of the compound to show the best binding with bacterial alanine racemase enzyme and block the biosynthesis of bacterial cell walls. Three compounds; Top-1, Top-2, and Top-3 with a binding affinity (in kcal/mol) of -8.7, -8.6, and -8.5, respectively were identified. The compounds were classified as good drug-like molecules as they clear parameters of Lipinski, Ghose Muegge, Vber, Egan, and MDDR drug-like rules. According to molecular dynamics simulation findings, the enzyme remained in good stable dynamics in the presence of compounds throughout the length of simulation time with average RMSD within the 3 Å range. Further observation noticed the enzyme residues in good overall stable behavior, particularly the active site residues. The intermolecular strength of interactions between the enzyme and compound was additionally cross-validated by binding free energy analysis. The net binding free energy (in kcal/mol) of Top-1, Top-2, and Top-3 is -22, -25.21, and -17, respectively in the MM-GBSA method and -32.14 (Top-1),-29.45 (Top-2) and -32.87 (Top-3) in WaterSwap. Together this study indicated the screened compounds as promising antibacterial and might be investigated in the experimental analysis for biological activity.</jats:p>
</jats:abstract>
<publication_date media_type="online">
<month>08</month>
<day>26</day>
<year>2024</year>
</publication_date>
<pages>
<first_page>1</first_page>
<last_page>12</last_page>
</pages>
<ai:program xmlns:ai="http://www.crossref.org/AccessIndicators.xsd" name="AccessIndicators">
<ai:license_ref>https://creativecommons.org/licenses/by-nc/4.0</ai:license_ref>
</ai:program>
<doi_data>
<doi>10.34091/ajls.v7i7.340</doi>
<resource>http://ajlifesciences.com/ojs/index.php/ajls/article/view/340</resource>
<collection property="crawler-based"/>
<collection property="text-mining"/>
</doi_data>
</journal_article>
</journal>
</body>
</doi_batch>