02364nas a2200193 4500008004100000022001400041245009200055210006900147260007100216300001400287490000700301520165100308100001601959700001801975700001701993700001702010700002202027856012102049 2012 eng d a1525-779700aSynthesis of silk fibroin-glycopolypeptide conjugates and their recognition with lectin0 aSynthesis of silk fibroinglycopolypeptide conjugates and their r a1155 16TH ST, NW, WASHINGTON, DC 20036 USAbAMER CHEMICAL SOCcNOV a3695-37020 v133 a

Silk fibroin (SF), the natural fibrous protein created by the Bombyx mori silk worm, is being increasingly excellent mechanical strength, high oxygen/water permeability, excellent mechanical strength; high oxygen/water:permeability, and biocompatibility: :It is also well known that surface. modification of SF, With Organic ligands such as the extracellular protein :binding. Arg-Gly-Asp, (RGD) peptides:,: help adhesion and,proliferation. of cells better-a key; requirement for it to function as extracellular. matrices; In this, Work, We have conjugated synthetic glycopolypeptides (GPs) that were synthesized by controlled ring opening polymerization of alpha-manno-lys N-carboxyanhydrides (NCAs) onto SF by using Cu catalyzed click reaction to synthesize 1 a new hybrid :Material (SF GP), Which We believe will have :both the mechanical properties of native SF and the molecular recognition property of the carbohydrates in the GP. By controlling the :amount of GP grafted onto SF, we have made three SF GP conjugates that differ in their ability to assemble into films. SF GP conjugates having a very high content of GP formed completely water soluble brush like polymer that displayed very high affinity toward the lectin concanavalin-A (Con-A) Films cast from SF-GP conjugates using lower amounts of grafted GP were more stable in water, and the stability can be modulated by varying the amount of G grafted. The water insoluble film SF-GP(25) was also found to bind to fluorescently labeled Con A, as was seen by confocal microscopy Such SF-GP hybrid films may be useful as mimics of extracellular matrices for tissue engineering:

1 aDas, Soumen1 aPati, Debasis1 aTiwari, Neha1 aNisal, Anuya1 aGupta, Sayam, Sen uhttps://library.ncl.res.in/content/synthesis-silk-fibroin-glycopolypeptide-conjugates-and-their-recognition-lectin-001601nas a2200169 4500008004100000022001400041245014800055210006900203260011000272300001400382490000600396520084900402100001601251700002001267700002201287856012201309 2013 eng d a1759-995400aSynthesis of end-functionalized phosphate and phosphonate-polypeptides by ring-opening polymerization of their corresponding N-carboxyanhydride0 aSynthesis of endfunctionalized phosphate and phosphonatepolypept aTHOMAS GRAHAM HOUSE, SCIENCE PARK, MILTON RD, CAMBRIDGE CB4 0WF, CAMBS, ENGLANDbROYAL SOC CHEMISTRYcAUG a4087-40910 v43 a

Phosphopolypeptides provide an interesting biomimetic analog for phosphorylated proteins that are involved in biomineralization. We have developed a high yielding synthesis of cysteine-based phosphate and phosphonate N-carboxyanhydride (NCA) by using the thiol-ene coupling reaction. These phosphate and phosphonate NCA monomers underwent polymerization using simple primary amine initiators to form well defined homophosphopolypeptides. Using a bifunctional initiator we were able to install a ``clickable'' alkyne or azide group at the end of the polypeptide chain. We were also able to successfully synthesize fully water-soluble phosphonate based polypeptides by hydrolysis of the corresponding phosphonate ester groups in the polypeptide. These water-soluble phosphopolypeptides adopt a random coil conformation at physiological pH.

1 aDas, Soumen1 aKar, Mrityunjoy1 aGupta, Sayam, Sen uhttps://library.ncl.res.in/content/synthesis-end-functionalized-phosphate-and-phosphonate-polypeptides-ring-opening-002193nas a2200253 4500008004100000022001400041245016500055210006900220260000800289300001400297490000700311520130700318653002201625653001201647653002401659653001301683653001801696100002001714700001601734700002001750700001801770700002201788856012901810 2020 eng d a2192-650600aSynthesis of phospho-polypeptides via phosphate-containing N-carboxyanhydride: application in enzyme-induced self-assembly, and calcium carbonate mineralization0 aSynthesis of phosphopolypeptides via phosphatecontaining Ncarbox cMAY a1053-10640 v853 a

An easy synthetic strategy was developed to synthesize the phosphate-functionalized amino acid N-carboxyanhydride (NCA), using simple primary amine initiators to obtain homo and block phospho-polypeptides with controlled molecular weight and molecular weight distribution. The methodology was extended to the synthesis of the end-functionalized homo polypeptides (15 to 50 repeat unit) and block co-polypeptides with PEG (0.7 K, 2 K, and 5 K) and glycopolypeptide (15-unit mannose glycopolypeptide) as one of the blocks. The deprotected fully water-soluble anionic phosphate-based polypeptides showed pH-dependent helical conformation with a helical content of 20 %, which further changed to beta-sheets upon addition of the enzyme alkaline phosphatase (ALP) due to dephosphorylation. The block co-polypeptide containing PEG as one of the blocks led to its self-assembly into colloidal structures, such as vesicles with a hydrodynamic diameter of similar to 250 nm, due to the formation of amphiphilic block co-polymer upon dephosphorylation. The nature of the colloidal structures formed can be temporally controlled by the extent of dephosphorylation. Finally, the phospho-polypeptides serve as a template for the mineralization of calcium carbonate with varying polymorphs and morphologies.

10aBiomineralization10aenzymes10aphosphopolypeptides10aProteins10aSelf-assembly1 aMondal, Basudeb1 aDas, Soumen1 aPanda, Sidharth1 aDutta, Tahiti1 aGupta, Sayam, Sen uhttps://library.ncl.res.in/content/synthesis-phospho-polypeptides-phosphate-containing-n-carboxyanhydride-application-enzyme