01975nas a2200205   4500008004100000022001400041245004300055210004300098260007300141300001200214490000600226520134100232653003901573653001801612653001301630100001901643700001701662700001501679856007501694       2005                        eng d  a1567-173900aInterfacing biology with nanoparticles0 aInterfacing biology with nanoparticles  aPO BOX 211, 1000 AE AMSTERDAM, NETHERLANDSbELSEVIER SCIENCE BVcFEB  a118-1270 v53 a<p>New approaches are constantly being developed for both the synthesis of inorganic nanomaterials and their surface modification for sensing and electronic applications. Insofar as surface modification of gold nanoparticles is concerned, thiol chemistry is the most popular approach to bind ligands to their surface. We have been pursuing the possibility of using amine functionality to bind ligands to the surface of gold nanoparticles and have found that amine binding is as strong as thiol binding. The advantages of using amine chemistry for surface modification of nanogold are many, the possibility of complexing a large variety of biomolecules such as amino acids and proteins being one of the most important. In this article, we review the work from this laboratory on the stabilization of gold nanoparticles using amino acids as well as using amino acids as reducing agents to obtain stable aqueous solutions of gold nanoparticles of variable size. We also discuss the possibility of forming bioconjugates of enzymes with gold nanoparticles decorating the surface of polymer microspheres and their application as reusable biocatalysts. There is much to be gained by marrying nanomaterials with biology with considerable spin-offs likely in both nanotechnology and biotechnology. (C) 2004 Elsevier B.V. All rights reserved.</p>10aamino acids' enzyme immobilization10aNanoparticles10aProteins1 aMandal, Sujata1 aPhadtare, S.1 aSastry, M.  uhttps://library.ncl.res.in/content/interfacing-biology-nanoparticles-002485nas a2200229   4500008004100000022001400041245014500055210006900200260008500269300001200354490000700366520159100373653002101964653001801985653001102003653001902014653001302033100003402046700002402080700002002104856013102124       2011                        eng d  a0032-389600aDevelopment of non-woven nanofibers of egg albumen-poly (vinyl alcohol) blends: influence of solution properties on morphology of nanofibers0 aDevelopment of nonwoven nanofibers of egg albumenpoly vinyl alco  a75 VARICK ST, 9TH FLR, NEW YORK, NY 10013-1917 USAbNATURE PUBLISHING GROUPcJUL  a654-6610 v433 a<p>Egg albumen (EA), a highly functional globular protein with desirable properties, is the least-explored material for biomaterial applications, although it is available in abundance. In our studies, we explored the viability of EA and various blends with biocompatible and non-toxic poly (vinyl alcohol) (PVA) to produce nanofibers for biomedical applications. EA and PVA blends were prepared in various compositions. Electrospinning was used to fabricate non-woven nanofibers. Solution properties, such as viscosity and electrical conductivity, were evaluated for various prepared solutions. Solution viscosity increased with increasing polymer concentration. Solutions with higher contents of EA recorded increased conductivity, which decreased with increasing PVA content. The influence of solution properties on the morphological appearance of as-spun products was studied using scanning electron microscopy. Instead of nanofibers, nanoparticles and microparticles of EA were produced at even higher contents. In contrast, a gradual increase in the addition of PVA content to 8% EA solution resulted in the transformation of particles from large agglomerates to very fine fibers (approximate to 100nm in diameter) because of the influence of polymer content, viscosity and conductivity. The polymer-polymer interactions in the prepared materials have been validated by Fourier transform infrared spectroscopy, differential scanning calorimetry, X-ray diffraction and gel electrophoresis. Polymer Journal (2011) 43, 654-661; doi:10.1038/pj.2011.34; published online 18 May 2011</p>10aBiocompatibility10abiodegradable10ablends10ananotechnology10aProteins1 aRathna, Gundloori, Venkata Na1 aJog, Jyoti, Prakash1 aGaikwad, A., B.  uhttps://library.ncl.res.in/content/development-non-woven-nanofibers-egg-albumen-poly-vinyl-alcohol-blends-influence-solution-001757nas a2200241   4500008004100000022001400041245008700055210006900142260007100211300001400282490000600296520090500302653002501207653002301232653002901255653001301284653001701297100002101314700001801335700002201353700002201375856011801397       2014                        eng d  a2168-048500aInvestigation of C-C bond formation mediated by bombyx mori silk fibroin materials0 aInvestigation of CC bond formation mediated by bombyx mori silk   a1155 16TH ST, NW, WASHINGTON, DC 20036 USAbAMER CHEMICAL SOCcJUN  a1510-15170 v23 a<p>The formation of C-C bonds is a prerequisite for all life on earth. Understanding the role of proteins in mediating the formation of these bonds is important for understanding biological mechanisms in evolution, as well as for designing ``green catalysts''. In this work, the ability of silk fibroin (SF) proteins to mediate selective C-C bond formation under mild conditions was comprehensively evaluated and compared between different SF-based materials and other proteins. Aqueous SF solution (ASFS), freeze-dried SF (FDSF), mesoporous SF (MPSF), and SF hydrogel (SFHG) materials were prepared and characterized by a variety of techniques including, among others, FE-SEM, ICP-OES, FT-IR, and TGA. The nitroaldol (Henry) reaction, Knoevenagel condensation, and direct aldol reaction were used as models for this study, in which the recovery and reusability of the protein was also evaluated.</p>10aAldol-like reactions10aC-C Bond formation10aKnoevenagel condensation10aProteins10aSilk fibroin1 aKuehbeck, Dennis1 aGhosh, Munmun1 aGupta, Sayam, Sen1 aDiaz, David, Diaz  uhttps://library.ncl.res.in/content/investigation-c-c-bond-formation-mediated-bombyx-mori-silk-fibroin-materials-002823nas a2200313   4500008004100000022001400041245009900055210006900154260000800223300001600231490000700247520186600254653001702120653001302137653001802150653001402168653003202182653001302214653001602227653001202243653001302255653001102268100002202279700002302301700001902324700002102343700001502364856013002379       2017                        eng d  a1463-907600aNature of selenium hydrogen bonding: gas phase spectroscopy and quantum chemistry calculations0 aNature of selenium hydrogen bonding gas phase spectroscopy and q  cSEP  a24179-241870 v193 a<div class="block-record-info" style="margin: 0px 22px 22px; list-style: none; padding: 0px; line-height: 20px; font-size: 13px; color: rgb(51, 51, 51); font-family: arial, helvetica, sans-serif; background-color: rgb(248, 248, 248);"><p class="FR_field" style="margin: 0px 0px 2px; list-style: none; padding: 0px; line-height: 22px;">Subsequent to the recent re-definition of hydrogen bonding by the IUPAC committee, there has been a growing search for finding the presence of this ever interesting non-covalent interaction between a hydrogen atom in an X-H group and any other atom in the periodic table. In recent gas phase experiments, it has been observed that hydrogen bonding interactions involving S and Se are of similar strength to those with an O atom. However, there is no clear explanation for the unusual strength of this interaction in the case of hydrogen bond acceptors which are not conventional electronegative atoms. In this work, we have explored the nature of Se hydrogen bonding by studying indole...dimethyl selenide (indmse) and phenol...dimethyl selenide (phdmse) complexes using gas phase IR spectroscopy and quantum chemistry calculations. We have found through various energy decomposition analysis (EDA) methods and natural bond orbital (NBO) calculations that, along with electrostatics and polarization, charge transfer interactions are important to understand Se/S hydrogen bonding and there is a delicate balance between the various interactions that plays the crucial role rather than a single component of the interaction energy. An in-depth understanding of this type of non-covalent interaction has immense significance in biology as amino acids containing S and Se are widely present in proteins and hence hydrogen bonding interactions involving S and Se atoms contribute to the folding of proteins.</p></div><p>&nbsp;</p>10aCenter-Dot-O10aClusters10aCo-Ordination10aComplexes10aintermolecular interactions10aProteins10aReplacement10aspectra10aStrength10aSulfur1 aMishra, Kamal, K.1 aSingh, Santosh, K.1 aGhosh, Paulami1 aGhosh, Debashree1 aDas, Aloke  uhttps://library.ncl.res.in/content/nature-selenium-hydrogen-bonding-gas-phase-spectroscopy-and-quantum-chemistry-calculations02210nas a2200277   4500008004100000022001300041245014900054210006900203260000900272300001600281490000600297520121800303653003101521653003401552653001801586653003701604653001301641653001301654653002201667653002201689653001501711653002301726100002201749700003101771856013001802       2018                        eng d  a2470134300aSurface modification of polymers for tissue engineering applications: arginine acts as a sticky protein equivalent for viable cell accommodation0 aSurface modification of polymers for tissue engineering applicat  cAPR   a4242–42510 v33 a<p>Hydrophobic polymers, for their favorable mechanical properties, are a popular choice as permanent bioimplants. These materials remain absolutely bioinert for years, but throw up challenges when it comes to fast integration with healthy tissue. Addressing this, herein, we present a surface-modification technique of converting the hydrophobic surface of a polymeric film into a hydrophilic one using a layer-by-layer assembly process involving gold nanoparticles and small molecules like amino acids. These films showed much improved animal cell (murine fibroblast) adherence properties compared to commercially available tissue culture plates. Moreover, arginine-modified films exhibited a nearly equivalent cell viability compared to the films modified with the natural extracellular matrix component fibronectin. The surface hydrophilicity and roughness of our novel film were characterized by contact angle measurement and atomic force microscopy. Cell counting, fluorescence microscopy, cell viability, and collagen estimation assay were employed to demonstrate that our film favored a much improved cell adherence, and accommodation in comparison to the commercially available tissue culture plates.</p>10aCell and Molecular biology10aExtracellular matrix proteins10aNanoparticles10aPhysical and chemical properties10aPolymers10aProteins10aSurface structure10aSurface treatment10aThin films10atissue engineering1 aSengupta, Poulomi1 aPrasad, Bhagavatula, L. V.  uhttps://library.ncl.res.in/content/surface-modification-polymers-tissue-engineering-applications-arginine-acts-sticky-protein02193nas 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<p>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.</p>
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