@article { ISI:000353167500032,
	title = {Sophorolipid assisted tunable and rapid gelation of silk fibroin to form porous biomedical scaffolds},
	journal = {RSC Advances},
	volume = {5},
	number = {43},
	year = {2015},
	month = {MAR},
	pages = {33955-33962},
	publisher = {ROYAL SOC CHEMISTRY},
	address = {THOMAS GRAHAM HOUSE, SCIENCE PARK, MILTON RD, CAMBRIDGE CB4 0WF, CAMBS, ENGLAND},
	abstract = {<p>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.</p>},
	issn = {2046-2069},
	doi = {10.1039/c5ra04317d},
	author = {Dubey, Parul and Nawale, Laxman and Sarkar, Dhiman and Nisal, Anuya and Prabhune, Asmita}
}
@article {45642,
	title = {Silk fibroin-sophorolipid gelation: deciphering the underlying mechanism},
	journal = {Biomacromolecules},
	volume = {17},
	year = {2016},
	month = {OCT},
	pages = {3318-3327},
	type = {Article},
	abstract = {<p>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.</p>},
	issn = {1525-7797},
	doi = {10.1021/acs.biomac.6b01069},
	author = {Dubey, Parul and Kumar, Sugam and Aswal, Vinod K. and Ravindranathan, Sapna and Rajamohanan, Pattuparambil R. and Prabhune, Asmita and Nisal, Anuya}
}
