01185nas a2200157 4500008004100000245010300041210006900144260005100213520053400264100001700798700001900815700001900834700001700853700002100870856013600891 2015 eng d00aMechanistic understanding of rapid gelation of silk fibroin using a biosurfactant – sophorolipid0 aMechanistic understanding of rapid gelation of silk fibroin usin aNational Chemical Laboratory, Pune IndiacFEB3 a

3D polymeric hydrogels find use in biomedical applications as scaffolds and drug delivery vehicle • Silk fibroin a structural protein is a promising candidate (excellent thermo-mechanicals, biocompatibility, biodegradability) • Sophorolipid (SL)-a biosurfactant is known to exhibit antimicrobial, anti cancerous and cell differentiating. • Use of SL as gelling agent can enhance the applicability of SF hydrogels • SF-SL scaffolds obtained by lyophilization of hydrogels can find application in tissue regeneration

1 aDubey, Parul1 aNawale, Laxman1 aSarkar, Dhiman1 aNisal, Anuya1 aPrabhune, Asmita uhttps://library.ncl.res.in/content/mechanistic-understanding-rapid-gelation-silk-fibroin-using-biosurfactant-%E2%80%93-sophorolipid01897nas a2200193 4500008004100000022001400041245010500055210006900160260011000229300001600339490000600355520112300361100001701484700001901501700001901520700001701539700002101556856012601577 2015 eng d a2046-206900aSophorolipid assisted tunable and rapid gelation of silk fibroin to form porous biomedical scaffolds0 aSophorolipid assisted tunable and rapid gelation of silk fibroin aTHOMAS GRAHAM HOUSE, SCIENCE PARK, MILTON RD, CAMBRIDGE CB4 0WF, CAMBS, ENGLANDbROYAL SOC CHEMISTRYcMAR a33955-339620 v53 a

Three dimensional polymer hydrogels, based on both natural and synthetic polymers, are increasingly being used as scaffolds and drug delivery vehicles for biomedical applications. Fibrous protein, silk fibroin (SF), obtained from the Bombyx mori silkworm is a promising candidate in this area. However, SF has a long gelation time of about a few weeks that can only be reduced by non-physiological treatments (e. g. high temperature, ultrasonication and low pH) or by addition of a chemical and non-biodegradable polymer and/or surfactant. We report here accelerated gelation of SF under physiological conditions using a biosurfactant, sophorolipid (SL) as a gelling agent. SL and SF are completely miscible and form a very clear solution upon mixing. Hence it is interesting to see that this clear solution gels in a time span of just a few hours. The hydrogels so formed have pore architecture, porosities and mechanical stability ideally suited for tissue culture applications. Here we also demonstrate that mouse fibroblast cells not only adhere to but also extensively proliferate on these SF-SL scaffolds.

1 aDubey, Parul1 aNawale, Laxman1 aSarkar, Dhiman1 aNisal, Anuya1 aPrabhune, Asmita uhttps://library.ncl.res.in/content/sophorolipid-assisted-tunable-and-rapid-gelation-silk-fibroin-form-porous-biomedical-001826nas a2200181 4500008004100000022001400041245012200055210006900177260011000246300001600356490000600372520105900378100002601437700002001463700001701483700002101500856012301521 2015 eng d a2046-206900aUV-assisted size sampling and antibacterial screening of lantana camara leaf extract synthesized silver nanoparticles0 aUVassisted size sampling and antibacterial screening of lantana  aTHOMAS GRAHAM HOUSE, SCIENCE PARK, MILTON RD, CAMBRIDGE CB4 0WF, CAMBS, ENGLANDbROYAL SOC CHEMISTRYcFEB a24513-245200 v53 a

Green route synthesized silver nanoparticles are extremely toxic to multidrug resistant bacteria and have widespread applications in biomedical science. If the silver reducing weed extract possesses antimicrobial properties then it can additionally contribute to the medicinal activity. Herein, we present a synthesis of silver nanoparticles by using the weed plant Lantana camara's leaf extract. This study shows an easy, quick and cost-effective route to silver nanoparticle synthesis. Size controlled synthesis of Ag-0 nanoparticles is studied and discussed based on optical absorption, photoluminescence, dynamic light scattering (DLS), zeta potential, infrared spectroscopy, X-ray diffraction measurements, FE-SEM and TEM analysis. The synthesis of silver nanoparticles via this green approach shows very high antibacterial activity against E coli (Gram -ve) and S. aureus (Gram +ve) bacteria at a very low concentration (50 ppm Ag nanoparticles). Use of such eco-friendly nanoparticles may open a door for a new range of bactericidal agents.

1 aSingh, Pradeep, Kumar1 aBhardwaj, Kirti1 aDubey, Parul1 aPrabhune, Asmita uhttps://library.ncl.res.in/content/uv-assisted-size-sampling-and-antibacterial-screening-lantana-camara-leaf-extract-001955nas a2200217 4500008004100000022001400041245007700055210006900132260000800201300001400209490000700223520124600230100001701476700001701493700002101510700002601531700003501557700002101592700001701613856010701630 2016 eng d a1525-779700aSilk fibroin-sophorolipid gelation: deciphering the underlying mechanism0 aSilk fibroinsophorolipid gelation deciphering the underlying mec cOCT a3318-33270 v173 a

Silk fibroin (SF) protein, produced by silkworm Bombyx mori, is a promising biomaterial, while sophorolipid (SL) is an amphiphilic functional biosurfactant synthesized by nonpathogenic yeast Candida bombicola. SL is a mixture of two forms, acidic (ASL) and lactonic (LSL), which when added to SF results in accelerated gelation of silk fibroin. LSL is known to have multiple biological functionalities and hence hydrogels of these green molecules have promising applications in the biomedical sector. In this work, SANS, NMR, and rheology are employed to examine the assembling properties of individual and mixed SLs and their interactions with SF to understand the mechanism that leads to rapid gelation. SANS and NMR studies show that ASL assembles to form charged micelles, while LSL forms micellar assemblies and aggregates of a mass fractal nature. ASL and LSL together form larger mixed micelles, all of which interact differently with SF. It is shown that preferential binding of LSL to SF causes rapid unfolding of the SF chain leading to the formation of intermolecular beta sheets, which trigger fast gelation. Based on the observations, a mechanism for gelation of SF in the presence of different sophorolipids is proposed.

1 aDubey, Parul1 aKumar, Sugam1 aAswal, Vinod, K.1 aRavindranathan, Sapna1 aRajamohanan, Pattuparambil, R.1 aPrabhune, Asmita1 aNisal, Anuya uhttps://library.ncl.res.in/content/silk-fibroin-sophorolipid-gelation-deciphering-underlying-mechanism02007nas a2200181 4500008004100000245012400041210006900165260000800234300001300242490000800255520133400263100001901597700001701616700002301633700001901656700002101675856012901696 2017 eng d00aAnti-proliferative effect of novel primary cetyl alcohol derived sophorolipids against human cervical cancer cells HeLa0 aAntiproliferative effect of novel primary cetyl alcohol derived  cAPR ae01742410 v12 3 aSophorolipids (SLs) are glycolipid biosurfactants that have been shown to display anticancer activity. In the present study, we report anti-proliferative studies on purified forms of novel SLs synthesized using cetyl alcohol as the substrate (referred as SLCA) and their anticancer mechanism in human cervical cancer cells. Antiproliferative effect of column purified SLCA fractions (A, B, C, D, E and F) was examined in panel of human cancer cell lines as well as primary cells. Among these fractions, SLCA B and C significantly inhibited the survival of HeLa and HCT 116 cells without affecting the viability of normal human umbilical vein endothelial cells (HUVEC). The two fractions were identified as cetyl alcohol sophorolipids with non-hydroxylated tail differing in the degree of acetylation on sophorose head group. At an IC50 concentration SLCA B (16.32 mu g ml(-1)) and SLCA C (14.14 mu g ml(-1)) blocked the cell cycle progression of HeLa cells at G1/S phase in time-dependent manner. Moreover, SLCA B and SLCA C induced apoptosis in HeLa cells through an increase in intracellular Ca2+ leading to depolarization of mitochondrial membrane potential and increase in the caspase-3, -8 and -9 activity. All these findings suggest that these SLCAs could be explored for their chemopreventive potential in cervical cancer.1 aNawale, Laxman1 aDubey, Parul1 aChaudhari, Bhushan1 aSarkar, Dhiman1 aPrabhune, Asmita uhttps://library.ncl.res.in/content/anti-proliferative-effect-novel-primary-cetyl-alcohol-derived-sophorolipids-against-human02000nas a2200301 4500008004100000022001400041245009700055210006900152260000900221300000900230490000800239520101400247653001501261653004401276653000701320653001701327653003501344653001701379100001701396700001701413700002601430700002201456700002101478700003501499700001701534700002101551856012601572 2018 eng d a0254-058400apH dependent sophorolipid assemblies and their influence on gelation of silk fibroin protein0 apH dependent sophorolipid assemblies and their influence on gela cJAN  a9-160 v2033 a

Sophorolipid (SL), a bio-derived surfactant is an excellent gelling agent for natural fibrous protein, silk fibroin (SF) leading to potential biomedical applications. Interaction of SF with SL has been shown to accelerate the formation of hydrogel with the rate being dependent on the form of SL used. Here, we examine the effect of pH on SL-SF interaction and gel formation by employing rheology, fluorescence spectroscopy, SANS and NMR. The results indicate that the size of SL assemblies decrease as pH increases from acidic to alkaline and significantly impacts the association of SL and SF. The association of SF and SL is mainly via hydrophobic interactions, with the SL molecules forming bead like structures along the SF chain. The increased charge on the acidic form of SL at higher pH results in greater repulsion between acidic SL molecules, which are bound to the hydrophobic sites of SF, leading to rapid chain unfolding and subsequent gelation. (C) 2017 Elsevier B.V. All rights reserved.

10aAssemblies10aNuclear magnetic resonance spectroscopy10apH10aSilk fibroin10aSmall angle neutron scattering10aSophorolipid1 aDubey, Parul1 aKumar, Sugam1 aRavindranathan, Sapna1 aVasudevan, Sahana1 aAswal, Vinod, K.1 aRajamohanan, Pattuparambil, R.1 aNisal, Anuya1 aPrabhune, Asmita uhttps://library.ncl.res.in/content/ph-dependent-sophorolipid-assemblies-and-their-influence-gelation-silk-fibroin-protein