Structural dynamics and modeling of curcin protein: docking against pterin derivatives
Jatropha species have been widely targeted for its use in oil and biodiesel production. The extraction of oil and biodiesel has been curbed due to the presence of curcin, a toxalbumin that can execute detailed toxic compounds . In silico approaches were undertaken to analyse the inhibition of curcin...
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| Veröffentlicht in: | SN applied sciences 2019-08, Vol.1 (8), p.812, Article 812 |
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| creator | Palanivel, Hemalatha Easwaran, Murugesh Meena, Arun Chandrasekaran, Suryanarayanan Abdul Kader, M. Murali, Adhigan |
| description | Jatropha
species have been widely targeted for its use in oil and biodiesel production. The extraction of oil and biodiesel has been curbed due to the presence of curcin, a toxalbumin that can execute detailed toxic compounds
. In silico
approaches were undertaken to analyse the inhibition of curcin via pterin inhibitors, which show the structural similarities to ricin inhibitors. The identification of actual residues of predicted active sites, involved in binding with the ligands was accurately confirmed by molecular docking analysis. Among the eleven ligands screened in the present study, particularly, the folic acid showed the maximum docking score, which confirmed their hydrophobic site, hydrogen-bond donor and hydrogen-bond acceptor of folic acid, which could render the optimal biological function through inhibition of curcin.
Graphic abstract |
| doi_str_mv | 10.1007/s42452-019-0752-5 |
| format | Article |
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species have been widely targeted for its use in oil and biodiesel production. The extraction of oil and biodiesel has been curbed due to the presence of curcin, a toxalbumin that can execute detailed toxic compounds
. In silico
approaches were undertaken to analyse the inhibition of curcin via pterin inhibitors, which show the structural similarities to ricin inhibitors. The identification of actual residues of predicted active sites, involved in binding with the ligands was accurately confirmed by molecular docking analysis. Among the eleven ligands screened in the present study, particularly, the folic acid showed the maximum docking score, which confirmed their hydrophobic site, hydrogen-bond donor and hydrogen-bond acceptor of folic acid, which could render the optimal biological function through inhibition of curcin.
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species have been widely targeted for its use in oil and biodiesel production. The extraction of oil and biodiesel has been curbed due to the presence of curcin, a toxalbumin that can execute detailed toxic compounds
. In silico
approaches were undertaken to analyse the inhibition of curcin via pterin inhibitors, which show the structural similarities to ricin inhibitors. The identification of actual residues of predicted active sites, involved in binding with the ligands was accurately confirmed by molecular docking analysis. Among the eleven ligands screened in the present study, particularly, the folic acid showed the maximum docking score, which confirmed their hydrophobic site, hydrogen-bond donor and hydrogen-bond acceptor of folic acid, which could render the optimal biological function through inhibition of curcin.
Graphic abstract</description><subject>Applied and Technical Physics</subject><subject>Binding sites</subject><subject>Biodiesel fuels</subject><subject>Biofuels</subject><subject>Chemistry/Food Science</subject><subject>Chemistry: Frontiers in Materials from Basic Science to Real-Time Applications</subject><subject>Diesel</subject><subject>Earth Sciences</subject><subject>Engineering</subject><subject>Environment</subject><subject>Folic acid</subject><subject>Hydrogen bonds</subject><subject>Hydrophobicity</subject><subject>Inhibitors</subject><subject>Ligands</subject><subject>Materials Science</subject><subject>Molecular docking</subject><subject>Petroleum production</subject><subject>Protein synthesis</subject><subject>Proteins</subject><subject>Research Article</subject><subject>Ricin</subject><subject>Seeds</subject><subject>Toxicity</subject><issn>2523-3963</issn><issn>2523-3971</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2019</creationdate><recordtype>article</recordtype><recordid>eNp1UMtKAzEUDaJgqf0AdwHXo8nNZJK4k-ILCi58bEMyk5SpbaYmmUL_3pSKrtzce-A87uUgdEnJNSVE3KQaag4VoaoiogB-gibAgVVMCXr6ixt2jmYprQghIBSrJZugj9ccxzaP0axxtw9m07cJm9DhzdC5dR-WePC4HWPbB7yNQ3Z9uMXd0H4eKLM0fUgZb7OLhe_K3Jnc71y6QGferJOb_ewpen-4f5s_VYuXx-f53aJqGaW5sh2l1teNAOKl5UCBWmsbooxqiLDSSKK4As9BqcbXglnfCe49KOk85ZZN0dUxt_z2NbqU9WoYYygnNQgpa5Agm6KiR1Ubh5Si83ob-42Je02JPjSojw3q0qA-NKh58cDRk4o2LF38S_7f9A2f-HOp</recordid><startdate>20190801</startdate><enddate>20190801</enddate><creator>Palanivel, Hemalatha</creator><creator>Easwaran, Murugesh</creator><creator>Meena, Arun</creator><creator>Chandrasekaran, Suryanarayanan</creator><creator>Abdul Kader, M.</creator><creator>Murali, Adhigan</creator><general>Springer International Publishing</general><general>Springer Nature B.V</general><scope>AAYXX</scope><scope>CITATION</scope><orcidid>https://orcid.org/0000-0003-2726-8085</orcidid></search><sort><creationdate>20190801</creationdate><title>Structural dynamics and modeling of curcin protein: docking against pterin derivatives</title><author>Palanivel, Hemalatha ; Easwaran, Murugesh ; Meena, Arun ; Chandrasekaran, Suryanarayanan ; Abdul Kader, M. ; Murali, Adhigan</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c311t-bd11bf46720f8b52121bbb609a9607b8a809592f52996f473bfd75ff298ef15b3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2019</creationdate><topic>Applied and Technical Physics</topic><topic>Binding sites</topic><topic>Biodiesel fuels</topic><topic>Biofuels</topic><topic>Chemistry/Food Science</topic><topic>Chemistry: Frontiers in Materials from Basic Science to Real-Time Applications</topic><topic>Diesel</topic><topic>Earth Sciences</topic><topic>Engineering</topic><topic>Environment</topic><topic>Folic acid</topic><topic>Hydrogen bonds</topic><topic>Hydrophobicity</topic><topic>Inhibitors</topic><topic>Ligands</topic><topic>Materials Science</topic><topic>Molecular docking</topic><topic>Petroleum production</topic><topic>Protein synthesis</topic><topic>Proteins</topic><topic>Research Article</topic><topic>Ricin</topic><topic>Seeds</topic><topic>Toxicity</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Palanivel, Hemalatha</creatorcontrib><creatorcontrib>Easwaran, Murugesh</creatorcontrib><creatorcontrib>Meena, Arun</creatorcontrib><creatorcontrib>Chandrasekaran, Suryanarayanan</creatorcontrib><creatorcontrib>Abdul Kader, M.</creatorcontrib><creatorcontrib>Murali, Adhigan</creatorcontrib><collection>CrossRef</collection><jtitle>SN applied sciences</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Palanivel, Hemalatha</au><au>Easwaran, Murugesh</au><au>Meena, Arun</au><au>Chandrasekaran, Suryanarayanan</au><au>Abdul Kader, M.</au><au>Murali, Adhigan</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Structural dynamics and modeling of curcin protein: docking against pterin derivatives</atitle><jtitle>SN applied sciences</jtitle><stitle>SN Appl. Sci</stitle><date>2019-08-01</date><risdate>2019</risdate><volume>1</volume><issue>8</issue><spage>812</spage><pages>812-</pages><artnum>812</artnum><issn>2523-3963</issn><eissn>2523-3971</eissn><abstract>Jatropha
species have been widely targeted for its use in oil and biodiesel production. The extraction of oil and biodiesel has been curbed due to the presence of curcin, a toxalbumin that can execute detailed toxic compounds
. In silico
approaches were undertaken to analyse the inhibition of curcin via pterin inhibitors, which show the structural similarities to ricin inhibitors. The identification of actual residues of predicted active sites, involved in binding with the ligands was accurately confirmed by molecular docking analysis. Among the eleven ligands screened in the present study, particularly, the folic acid showed the maximum docking score, which confirmed their hydrophobic site, hydrogen-bond donor and hydrogen-bond acceptor of folic acid, which could render the optimal biological function through inhibition of curcin.
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| ispartof | SN applied sciences, 2019-08, Vol.1 (8), p.812, Article 812 |
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| language | eng |
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| source | Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals |
| subjects | Applied and Technical Physics Binding sites Biodiesel fuels Biofuels Chemistry/Food Science Chemistry: Frontiers in Materials from Basic Science to Real-Time Applications Diesel Earth Sciences Engineering Environment Folic acid Hydrogen bonds Hydrophobicity Inhibitors Ligands Materials Science Molecular docking Petroleum production Protein synthesis Proteins Research Article Ricin Seeds Toxicity |
| title | Structural dynamics and modeling of curcin protein: docking against pterin derivatives |
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