Biophysical characterization of aquaporins of aedes aegypti mosquito

dc.contributor.guideKavitha sankaranarayanan
dc.coverage.spatialBiophysical characterization of Aquaporins of aedes aegypti mosquito
dc.creator.researcherSandhya sreedharan K V
dc.date.accessioned2019-08-20T10:17:13Z
dc.date.available2019-08-20T10:17:13Z
dc.date.awarded30/05/2018
dc.date.completed2018
dc.date.registeredn.d.
dc.description.abstractAquaporins (AQPs) are transmembrane channels expressed in newlinealmost all the living organisms. AQPs facilitate efficient and selective newlinetransport of water across biological membranes, while related newlineaquaglyceroporins are additionally permeated by small neutral solutes such as newlineglycerol and urea. Since their discovery in 1992 AQPs have been gaining so newlinemuch importance in the research field. They have been recently suggested to newlinebe an active target to be tapped for the development of effective insecticides. newlineFor the present thesis we employed both in-silico methods and in-vitro newlineanalysis to characterize AQPs of Aedes aegypti, a mosquito vector responsible newlinefor the transmission of deadly diseases such as dengue and Zika viral newlineinfection. At first, we assessed the compatibility of putative AQPs in newlineA.aegypti (AQP1 to AQP6) for water transport and also identified the unique newlinechannel lining residues which can be considered as insect specific. The newlineanalysis reveal that the residues in the aromatic/arginine (ar/R) selectivity newlinefilter and the conducting pore in AQP1 is exactly similar to orthodox newlinemammalian AQPs, while AQP2 has a substitution at LE1position possibly newlinemaking it less efficient in high capacity water transport. The huge difference newlinein the selectivity filter region of AQP3 suggests a different transport property newlinefor this channel. The changes observed in the H5 position of the filter of newlineAQP4 and AQP5 may explain the presence of a larger pore aperture to permit newlinethe passage of larger solute molecules. AQP6 has divergent NPA motif and it newlinepossesses a completely hydrophobic filter region sharing similarity with newlinemammalian super aquaporins. newline newline
dc.description.note
dc.format.accompanyingmaterialNone
dc.format.dimensions21cm
dc.format.extentxvii, 140p.
dc.identifier.urihttp://hdl.handle.net/10603/253153
dc.languageEnglish
dc.publisher.institutionFaculty of Science and Humanities
dc.publisher.placeChennai
dc.publisher.universityAnna University
dc.relationp.125-139
dc.rightsuniversity
dc.source.universityUniversity
dc.subject.keywordaedes aegypti
dc.subject.keywordmosquito
dc.subject.keywordPhysical Sciences,Physics,Physics Applied
dc.titleBiophysical characterization of aquaporins of aedes aegypti mosquito
dc.title.alternative
dc.type.degreePh.D.

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