Biochemical and computational insights of adenosine deaminase inhibition by Epigallocatechin gallate
[Display omitted] •Adenosine deaminase inhibitory activity of Epigallocatechin gallate is evaluated.•Inhibition assay indicated that the compound significantly reduced ADA activity.•As per ITC data, the binding free energy is −6.84 Kcal mol−1.•The binding is also confirmed by fluorescence spectromet...
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| Veröffentlicht in: | Computational biology and chemistry 2019-12, Vol.83, p.107111-107111, Article 107111 |
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| container_title | Computational biology and chemistry |
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| creator | K.G, Arun C.S, Sharanya J, Abhithaj C, Sadasivan |
| description | [Display omitted]
•Adenosine deaminase inhibitory activity of Epigallocatechin gallate is evaluated.•Inhibition assay indicated that the compound significantly reduced ADA activity.•As per ITC data, the binding free energy is −6.84 Kcal mol−1.•The binding is also confirmed by fluorescence spectrometry study.•In silico studies revealed the structural details of binding.
Epigallocatechin gallate, a flavonoid from Camellia sinensis possess various pharmacological activities such as anticancer, antimicrobial and antioxidant etc. Adenosine deaminase, (ADA), is a key enzyme involved in the purine metabolism, the inhibitors of which is being considered as highly promising candidate for the development of anti-proliferative and anti-inflammatory drugs. In this work we studied adenosine deaminase inhibitory activity of epigallocatechin gallate by using biophysical and computational methods. The enzyme inhibition study result indicated that epigallocatechin gallate possess strong inhibitory activity on ADA. ITC study revealed the energetics of binding. Also the binding is confirmed by using fluorescence spectroscopy. The structural details of binding are obtained from molecular docking and MD simulation studies. |
| doi_str_mv | 10.1016/j.compbiolchem.2019.107111 |
| format | Article |
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•Adenosine deaminase inhibitory activity of Epigallocatechin gallate is evaluated.•Inhibition assay indicated that the compound significantly reduced ADA activity.•As per ITC data, the binding free energy is −6.84 Kcal mol−1.•The binding is also confirmed by fluorescence spectrometry study.•In silico studies revealed the structural details of binding.
Epigallocatechin gallate, a flavonoid from Camellia sinensis possess various pharmacological activities such as anticancer, antimicrobial and antioxidant etc. Adenosine deaminase, (ADA), is a key enzyme involved in the purine metabolism, the inhibitors of which is being considered as highly promising candidate for the development of anti-proliferative and anti-inflammatory drugs. In this work we studied adenosine deaminase inhibitory activity of epigallocatechin gallate by using biophysical and computational methods. The enzyme inhibition study result indicated that epigallocatechin gallate possess strong inhibitory activity on ADA. ITC study revealed the energetics of binding. Also the binding is confirmed by using fluorescence spectroscopy. The structural details of binding are obtained from molecular docking and MD simulation studies.</description><identifier>ISSN: 1476-9271</identifier><identifier>EISSN: 1476-928X</identifier><identifier>DOI: 10.1016/j.compbiolchem.2019.107111</identifier><identifier>PMID: 31445420</identifier><language>eng</language><publisher>England: Elsevier Ltd</publisher><subject>Adenosine deaminase ; Adenosine Deaminase - metabolism ; Adenosine Deaminase Inhibitors - chemistry ; Adenosine Deaminase Inhibitors - pharmacology ; Calorimetry ; Camellia sinensis - chemistry ; Catechin - analogs & derivatives ; Catechin - chemistry ; Catechin - pharmacology ; Epigallocatechin gallate ; Fluorescence spectroscopy ; Humans ; ITC ; Molecular Docking Simulation ; Molecular dynamics ; Molecular Dynamics Simulation ; Spectrometry, Fluorescence ; Thermodynamics</subject><ispartof>Computational biology and chemistry, 2019-12, Vol.83, p.107111-107111, Article 107111</ispartof><rights>2019 Elsevier Ltd</rights><rights>Copyright © 2019 Elsevier Ltd. All rights reserved.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c380t-20e00d89b38e54a5c651d3c92fafd0a8ac3fcfecd02885c24d698d69bfcf94a03</citedby><cites>FETCH-LOGICAL-c380t-20e00d89b38e54a5c651d3c92fafd0a8ac3fcfecd02885c24d698d69bfcf94a03</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S147692711830567X$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3537,27901,27902,65534</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/31445420$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>K.G, Arun</creatorcontrib><creatorcontrib>C.S, Sharanya</creatorcontrib><creatorcontrib>J, Abhithaj</creatorcontrib><creatorcontrib>C, Sadasivan</creatorcontrib><title>Biochemical and computational insights of adenosine deaminase inhibition by Epigallocatechin gallate</title><title>Computational biology and chemistry</title><addtitle>Comput Biol Chem</addtitle><description>[Display omitted]
•Adenosine deaminase inhibitory activity of Epigallocatechin gallate is evaluated.•Inhibition assay indicated that the compound significantly reduced ADA activity.•As per ITC data, the binding free energy is −6.84 Kcal mol−1.•The binding is also confirmed by fluorescence spectrometry study.•In silico studies revealed the structural details of binding.
Epigallocatechin gallate, a flavonoid from Camellia sinensis possess various pharmacological activities such as anticancer, antimicrobial and antioxidant etc. Adenosine deaminase, (ADA), is a key enzyme involved in the purine metabolism, the inhibitors of which is being considered as highly promising candidate for the development of anti-proliferative and anti-inflammatory drugs. In this work we studied adenosine deaminase inhibitory activity of epigallocatechin gallate by using biophysical and computational methods. The enzyme inhibition study result indicated that epigallocatechin gallate possess strong inhibitory activity on ADA. ITC study revealed the energetics of binding. Also the binding is confirmed by using fluorescence spectroscopy. The structural details of binding are obtained from molecular docking and MD simulation studies.</description><subject>Adenosine deaminase</subject><subject>Adenosine Deaminase - metabolism</subject><subject>Adenosine Deaminase Inhibitors - chemistry</subject><subject>Adenosine Deaminase Inhibitors - pharmacology</subject><subject>Calorimetry</subject><subject>Camellia sinensis - chemistry</subject><subject>Catechin - analogs & derivatives</subject><subject>Catechin - chemistry</subject><subject>Catechin - pharmacology</subject><subject>Epigallocatechin gallate</subject><subject>Fluorescence spectroscopy</subject><subject>Humans</subject><subject>ITC</subject><subject>Molecular Docking Simulation</subject><subject>Molecular dynamics</subject><subject>Molecular Dynamics Simulation</subject><subject>Spectrometry, Fluorescence</subject><subject>Thermodynamics</subject><issn>1476-9271</issn><issn>1476-928X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2019</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkMtO6zAQhi10EPdXQBGrs2kZO0nrsONSLhISG5DYWc54QqdK7BKnSLw9jgroLM_C8lz--cf-hDiTMJUgZ-erKYZuXXNocUndVIGsUmMupdwRB7KYzyaV0q9_fuO53BeHMa4AVA5Q7on9XBZFWSg4EO6Kw-jCaNvMepeN1pvBDhx8qrCP_LYcYhaazDryIbKnzJHt2NtIqb_kmkdxVn9mizW_2bYNaAfCJftszFJ8LHYb20Y6-b6PxMvt4vn6fvL4dPdwffk4wVzDMFFAAE5Xda6pLGyJs1K6HCvV2MaB1RbzBhtCB0rrElXhZpVOp07VqrCQH4m_W991H943FAfTcURKb_AUNtEopaEs82peJOnFVop9iLGnxqx77mz_aSSYkbJZmX8pm5Gy2VJOw6ffezZ1R-539AdrEtxsBZR--8HUm4hMHslxTzgYF_h_9nwB5xqXnQ</recordid><startdate>201912</startdate><enddate>201912</enddate><creator>K.G, Arun</creator><creator>C.S, Sharanya</creator><creator>J, Abhithaj</creator><creator>C, Sadasivan</creator><general>Elsevier Ltd</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>201912</creationdate><title>Biochemical and computational insights of adenosine deaminase inhibition by Epigallocatechin gallate</title><author>K.G, Arun ; C.S, Sharanya ; J, Abhithaj ; C, Sadasivan</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c380t-20e00d89b38e54a5c651d3c92fafd0a8ac3fcfecd02885c24d698d69bfcf94a03</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2019</creationdate><topic>Adenosine deaminase</topic><topic>Adenosine Deaminase - metabolism</topic><topic>Adenosine Deaminase Inhibitors - chemistry</topic><topic>Adenosine Deaminase Inhibitors - pharmacology</topic><topic>Calorimetry</topic><topic>Camellia sinensis - chemistry</topic><topic>Catechin - analogs & derivatives</topic><topic>Catechin - chemistry</topic><topic>Catechin - pharmacology</topic><topic>Epigallocatechin gallate</topic><topic>Fluorescence spectroscopy</topic><topic>Humans</topic><topic>ITC</topic><topic>Molecular Docking Simulation</topic><topic>Molecular dynamics</topic><topic>Molecular Dynamics Simulation</topic><topic>Spectrometry, Fluorescence</topic><topic>Thermodynamics</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>K.G, Arun</creatorcontrib><creatorcontrib>C.S, Sharanya</creatorcontrib><creatorcontrib>J, Abhithaj</creatorcontrib><creatorcontrib>C, Sadasivan</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Computational biology and chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>K.G, Arun</au><au>C.S, Sharanya</au><au>J, Abhithaj</au><au>C, Sadasivan</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Biochemical and computational insights of adenosine deaminase inhibition by Epigallocatechin gallate</atitle><jtitle>Computational biology and chemistry</jtitle><addtitle>Comput Biol Chem</addtitle><date>2019-12</date><risdate>2019</risdate><volume>83</volume><spage>107111</spage><epage>107111</epage><pages>107111-107111</pages><artnum>107111</artnum><issn>1476-9271</issn><eissn>1476-928X</eissn><abstract>[Display omitted]
•Adenosine deaminase inhibitory activity of Epigallocatechin gallate is evaluated.•Inhibition assay indicated that the compound significantly reduced ADA activity.•As per ITC data, the binding free energy is −6.84 Kcal mol−1.•The binding is also confirmed by fluorescence spectrometry study.•In silico studies revealed the structural details of binding.
Epigallocatechin gallate, a flavonoid from Camellia sinensis possess various pharmacological activities such as anticancer, antimicrobial and antioxidant etc. Adenosine deaminase, (ADA), is a key enzyme involved in the purine metabolism, the inhibitors of which is being considered as highly promising candidate for the development of anti-proliferative and anti-inflammatory drugs. In this work we studied adenosine deaminase inhibitory activity of epigallocatechin gallate by using biophysical and computational methods. The enzyme inhibition study result indicated that epigallocatechin gallate possess strong inhibitory activity on ADA. ITC study revealed the energetics of binding. Also the binding is confirmed by using fluorescence spectroscopy. The structural details of binding are obtained from molecular docking and MD simulation studies.</abstract><cop>England</cop><pub>Elsevier Ltd</pub><pmid>31445420</pmid><doi>10.1016/j.compbiolchem.2019.107111</doi><tpages>1</tpages></addata></record> |
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| subjects | Adenosine deaminase Adenosine Deaminase - metabolism Adenosine Deaminase Inhibitors - chemistry Adenosine Deaminase Inhibitors - pharmacology Calorimetry Camellia sinensis - chemistry Catechin - analogs & derivatives Catechin - chemistry Catechin - pharmacology Epigallocatechin gallate Fluorescence spectroscopy Humans ITC Molecular Docking Simulation Molecular dynamics Molecular Dynamics Simulation Spectrometry, Fluorescence Thermodynamics |
| title | Biochemical and computational insights of adenosine deaminase inhibition by Epigallocatechin gallate |
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