Triphenylamine and carbazole based donor Acceptor systems for Dye Sensitized solar cell Bio Imaging and sensor applications

Abstract

Podocytes are crucial cells of the glomerular filtration unit and playing a vital role newlineat the interface of the blood-urine barrier. Podocyte slit-diaphragm is a modified tight newlinejunction that facilitates size and charge-dependent permselectivity. Several proteins newlineincluding podocin, nephrin, CD2AP, and TRPC6 form a macromolecular assembly and newlineconstitute the slit-diaphragm (SD). The integrity of the SD depends on the interactions newlineamong the proteins involved in the macromolecular complexes with the key players being newlinenephrin, CD2AP, podocin, and TRPC6. Interestingly, the orthologs of the key SD proteins newlineare also involved in the similar complex formation and related functions suggesting an newlineevolutionary relationship between the invertebrate orthologs and vertebrate SD proteins. newlineWe, therefore, studied the evolution of nephrin, CD2AP, podocin, and TRPC6 proteins. newlineSeveral studies indicate that mutations cause severe damage to the SD structure which newlineleads to severe proteinuria. But the structural insights of how these proteins interact to newlineform complex assembly and how mutations alter these interactions remain poorly newlineunderstood. It has long been an interest of our laboratory to decipher the structural newlinefeatures and thermodynamic properties of the key SD proteins as the structural details of newlinethese proteins remain elusive. Greater understanding of SD architecture is limited by lack newlineof structural details of the proteins that constitute SD. Trying to specifically address these newlineintriguing questions, the following observations have been made as a part of my doctoral newlinework. An intense investigation has been carried out to study the structure of major SD newlineproteins, but we were successful in detailing podocin only. newline