02126nas a2200217   4500008004100000022001400041245009900055210006900154260007100223300001400294490000700308520131800315100001801633700002201651700001601673700002601689700002101715700002001736700002201756856013001778       2012                        eng d  a1525-779700aControlled synthesis of O-glycopolypeptide polymers and their molecular recognition by lectins0 aControlled synthesis of Oglycopolypeptide polymers and their mol  a1155 16TH ST, NW, WASHINGTON, DC 20036 USAbAMER CHEMICAL SOCcMAY  a1287-12950 v133 a<p>The facile synthesis of high molecular weight water-soluble O-glycopolypeptide polymers by the ring-opening polymerization of their corresponding N-carboxyanhydride (NCA) in very high yield (overall yield &gt; 70%) is reported. The per-acetylated-O-glycosylated lysine-NCA monomers, synthesized using stable glycosyl donors and a commercially available protected amino acid in very high yield, was polymerized using commercially available amine initiators. The synthesized water-soluble glycopolypeptides were found to be alpha-helical in aqueous solution. However, we were able to control the secondary conformation of the glycopolypeptides (alpha-helix vs nonhelical structures) by polymerizing raceznic amino acid glyco NCAs. We have also investigated the binding of the glycopolypeptide poly(alpha-manno-O-lys) with the lectin Con-A using precipitation and hemagglutination assays as well as by isothermal titration calorimetry (ITC). The ITC results clearly show that the binding process is enthalpy driven for both alpha-helical and nonhelical structures, with negative entropic contribution. Binding stoichiometry for the glycopolypeptide poly(alpha-manno-O-lys) having a nonhelical structure was slightly higher as compared to the corresponding polypeptide which adopted an alpha-helical structure.</p>1 aPati, Debasis1 aShaikh, Ashif, Y.1 aDas, Soumen1 aNareddy, Pavan, Kumar1 aSwamy, Musti, J.1 aHotha, Srinivas1 aGupta, Sayam, Sen  uhttps://library.ncl.res.in/content/controlled-synthesis-o-glycopolypeptide-polymers-and-their-molecular-recognition-lectins-0