02404nas a2200229   4500008004100000022001400041245016300055210006900218260007500287300001400362490000700376520146300383653002201846653002101868653001101889653004301900653002901943100002301972700002501995700002602020856012802046       2013                        eng d  a1053-050900aKinetics and thermodynamics of glycans and glycoproteins binding to holothuria scabra lectin: a fluorescence and surface plasmon resonance spectroscopic study0 aKinetics and thermodynamics of glycans and glycoproteins binding  a233 SPRING ST, NEW YORK, NY 10013 USAbSPRINGER/PLENUM PUBLISHERScNOV  a1147-11550 v233 a<p>Holothuria scabra produces a monomeric lectin (HSL) of 182 kDa. HSL showed strong antibacterial activity and induced bacterial agglutination under in vitro conditions, indicating its role in animals' innate immune responses. Very few lectins have been reported from echinoderms and none of these lectins have been explored in detail for their sugar-binding kinetics. Affinity, kinetics and thermodynamic analysis of glycans and glycoproteins binding to HSL were studied by fluorescence and surface plasmon resonance spectroscopy. Lectin binds with higher affinity to O-linked than N-linked asialo glycans, and the affinities were relatively higher than that for sialated glycans and glycoproteins. T-antigen alpha-methyl glycoside was the most potent ligand having the highest affinity (Ka 8.32 x10(7) M-1). Thermodynamic and kinetic analysis indicated that the binding of galactosyl Tn-antigen and asialo glycans is accompanied by an enthalpic contribution in addition to higher association rate coupled by low activation energy for the association process. Presence of sialic acid or protein matrix inhibits binding. Higher affinity of HSL for O-glycans than N-glycans had biological implications; since HSL specifically recognizes bacteria, which have mucin or O-glycan cognate on their cell surfaces and play a major role in animal innate immunity. Since, HSL had higher affinity to T-antigen, makes it a useful tool for cancer diagnostic purpose.</p>10aHolothuria scabra10aKinetic analysis10aLectin10aSurface plasmon resonance spectroscopy10aThermodynamic properties1 aGowda, Nagaraj, M.1 aGaikwad, Sushama, M.1 aKhan, Mohammad, Islam  uhttps://library.ncl.res.in/content/kinetics-and-thermodynamics-glycans-and-glycoproteins-binding-holothuria-scabra-lectin-002220nas a2200241   4500008004100000022001400041245012000055210006900175260000900244300001200253490000800265520138800273653001701661653001901678653001101697653001901708653002301727653002401750100002801774700002101802700002501823856013001848       2019                        eng d  a0003-986100aInvestigation of structural and saccharide binding transitions of Bauhinia purpurea and Wisteria floribunda lectins0 aInvestigation of structural and saccharide binding transitions o  cFEB   a134-1420 v6623 a<p>Two novel medicinally important legume lectins from Bauhinia purpurea (BPL) and Wisteria floribunda (WFL) possessing extended sugar binding site were investigated for functional and conformational transitions using biochemical and biophysical techniques as well as bioinformatical tools. Homology model of BPL was constructed using the Schrodinger suite and docked with N-acetyl galactosamine and T-antigen disaccharide (Gal beta 1-3GalNAc alpha O-Me). The longer loop D in the structure of WFL compared to that in BPL was found to be responsible for its specificity to LacdiNac (beta-D-GalNAc-[1 -&gt; 4]-DGlcNAc) over Gal beta 1-3GalNAc. BPL remained functionally stable up to 40 degrees C whereas WFL remained stable upto 70 degrees C indicating the strength of the sugar binding site geometry. Both the lectins showed intense but non-specific secondary structure in the range of 65-90 degrees C. WFL showed rapid aggregation above 80 degrees C as indicated by light scattering intensity. The lectins showed simultaneous dissociation and multistate unfolding in the vicinity of GdnHCl. At pH 1.0, both the lectins exhibited molten globule like structures, which were characterized further and were found to respond in a different way towards denaturants. The results have provided valuable insights into the molecular basis of the activity and stability of the two lectins.</p>10aConformation10aHomology model10aLectin10aMolten globule10asaccharide binding10aThermal aggregation1 aAgrawal, Sanskruthi, B.1 aGhosh, Deepanjan1 aGaikwad, Sushama, M.  uhttps://library.ncl.res.in/content/investigation-structural-and-saccharide-binding-transitions-bauhinia-purpurea-and-wisteria