02087nas a2200193   4500008004100000022001400041245006800055210006700123260007100190300001400261490000700275520140500282100002001687700002201707700002001729700002001749700002201769856010201791       2013                        eng d  a0743-746300aSynthesis and self-assembly of amphiphilic homoglycopolypeptide0 aSynthesis and selfassembly of amphiphilic homoglycopolypeptide  a1155 16TH ST, NW, WASHINGTON, DC 20036 USAbAMER CHEMICAL SOCcMAY  a5659-56670 v293 a<p>The synthesis of the amphiphilic homoglycopolypeptide was carried out by a combination of NCA polymerization and click chemistry to yield a well-defined Polypeptide having an amphiphilic carbohydrate on its side chain. The amphiphilicity of the carbohydrate was achieved by incorporation of an alkyl chain, at the C-6 position of the carbohydrate thus also rendering the homoglycopolypeptide amphiphilic. The homoglycopolypeptide formed multimicellar aggregates in water above a critical concentration of 0.9 mu M due to phase separation. The multimicellar aggregates were characterized by DLS, TEM, and AFM. It is proposed that hydrophobic interactions of the aliphatic chains at the 6-position of the sugar moieties drives the assembly of these rod-like homoglycopolypeptide into large;spherical aggregates. These multimicellar aggregates encapsulate both hydrophilic as well as hydrophobic dye as was confirmed by confocal microscopy. finally, amphiphilic random polypeptides containing 10% and 20% alpha-D-mannose in addition to glucose containing a, hydrophobic alkyl chain at its 6 position were synthesized by our methodology, and these polymers Were also found to assemble into spherical nanostructures. The spherical assemblies Of amphiphilic random glycopolypeptides containing 10% and 20% mannose were found to be surface bioactive and were found, to interact with the lectin Con-A.</p>1 aDhaware, Vinita1 aShaikh, Ashif, Y.1 aKar, Mrityunjoy1 aHotha, Srinivas1 aGupta, Sayam, Sen  uhttps://library.ncl.res.in/content/synthesis-and-self-assembly-amphiphilic-homoglycopolypeptide-0