Corrigendum to “Interaction between gallotannin and a recombinant form of arginine kinase of Trypanosoma brucei (TbAK): Thermodynamic and spectrofluorimetric evaluation”

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dc.contributor.authorAdeyemi, Oluyomi Stephen
dc.contributor.authorSulaiman, Adenike Faoziyat
dc.contributor.authorIniaghe, Martin Onome
dc.date.accessioned2020-01-24T12:11:27Z
dc.date.available2020-01-24T12:11:27Z
dc.date.issued2014
dc.descriptionData revealed inhibitory interactions between gallotannin and rTbAK. To our knowledge, this is the first report demonstrating the inhibitory potentials of gallotannin on the activity of rTbAK. The inhibitory relationships were consistent with noncompetitive interactions. Furthermore, the Stern-Volmer plots indicated that interactions involving the gallotannin, which caused the quenching of fluorescence intensity of the rTbAK,may be static.This is supported by the FRET analysis which also implicates the high probability for fluorescence exchange between rTBAK and gallotannin. Although the mechanism of inhibition is not clear yet, evidence presented warrants further kinetic analysis including molecular docking in order to clearly define the inhibitory interactions between the gallotannin and rTbAK.Theinsights of the binding properties have become necessary if selective inhibition of TbAK and eventual better trypanocides are desirable.en_US
dc.description.abstractCurrent chemotherapies against trypanosomiasis are beset with diverse challenges, a situation which underscores the numerous research efforts aimed at finding newer and effective treatments. Arginine kinase of trypanosome has been validated as target for drug development against trypanosomiasis. The present study investigated the interaction between a recombinant form of the arginine kinase (rTbAK) of trypanosome and gallotannin. The interaction between gallotannin and recombinant arginine kinase of Trypanosoma brucei caused significant decrease of enzyme activity. Kinetic analysis revealed the interaction to be of noncompetitive inhibition. Further thermodynamic analysis showed that the interaction between gallotannin and the recombinant arginine kinase was nonspontaneous and involved hydrophobic forces. The 𝐾sv values and the FRET analysis suggest that static quenching of fluorescence intensity by gallotannin was static.Data revealed inhibitory interactions between gallotannin and rTbAK of trypanosome. Although themechanism of inhibition is not clear yet, molecular docking studies are ongoing to clearly define the inhibitory interactions between the gallotannin and rTbAK.The knowledge of such binding properties would enrich development of selective inhibitors for the arginine kinase of Trypanosoma brucei.en_US
dc.description.sponsorshipAuthors appreciate Professor Whiteley at the Department of Biochemistry, Microbiology and Biotechnology, Rhodes University, South Africa.en_US
dc.identifier.citationAdeyemi Oluyomi Stephen, Sulaiman Adenike Faoziyat & Iniaghe Martin Onome (2018): Corrigendum to “Interaction between gallotannin and a recombinant form of arginine kinase of Trypanosoma brucei (TbAK): Thermodynamic and spectrofluorimetric evaluation”. Published by Hindawi Publishing Corporation in Journal of Biophysics, Article ID 1914746, Volume 2018: 1-7. Available online at https://www.hindawi.com/journals/jbp/2018/1914746/; http://dx.doi.org/10.1155/2014/675905;en_US
dc.identifier.otherArticle ID 675905
dc.identifier.urihttp://hdl.handle.net/123456789/3569
dc.language.isoen_USen_US
dc.publisherublished by Hindawi Publishing Corporation in Journal of Biophysicsen_US
dc.subjectGallotanninen_US
dc.subjectArginine Kinaseen_US
dc.subjectTrypanosoma bruceien_US
dc.subjectSpectrofluorimetric Evaluationen_US
dc.titleCorrigendum to “Interaction between gallotannin and a recombinant form of arginine kinase of Trypanosoma brucei (TbAK): Thermodynamic and spectrofluorimetric evaluation”en_US
dc.typeArticleen_US

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