@conference { ISI:000257623000188,
	title = {Gelation of regenerated fibroin solution},
	booktitle = {15th International Congress on Rheology/80th Annual Meeting of the Society-of-Rheology},
	series = {AIP CONFERENCE PROCEEDINGS},
	volume = {1027},
	year = {2008},
	note = {15th International Congress on Rheology/80th Annual Meeting of the Society-of-Rheology, Monterey, CA, AUG 03-08, 2008},
	month = {AUG},
	pages = {573-575},
	publisher = {Amer Inst Physics, 2 Huntington Quadrangle, STE 1NO1, Melville, NY 11747-4501 USA},
	organization = {Amer Inst Physics, 2 Huntington Quadrangle, STE 1NO1, Melville, NY 11747-4501 USA},
	address = {Monterey, CA.},
	abstract = {<p>Silk fibroin is a high molecular weight multiblock ampiphillic protein known for its ability to form high strength fibers. It is also biocompatible; silk sutures have been traditionally used for many centuries. Recently, there has been much interest in making silk hydrogels for applications ranging from tissue engineering to controlled delivery. Fibroin gels can be formed from aqueous solutions by changing one or more state variables such as pH, temperature and ionic strength. In this work we present our investigations on the gelation of aqueous fibroin solutions derived from Bombyx Mori silk using light scattering, confocal microscopy and rheological techniques.</p>},
	keywords = {dynamic light scattering, Rheology, silk fibroin gel},
	isbn = {978-0-7354-0549-3},
	issn = {0094-243X},
	author = {Nagarkara, Shailesh and Lele, Ashish K. and Chassenieux, Christophe and Nicolai, Taco and Durand, Dominique},
	editor = {Co, A. and Leal, L. G. and Colby, R. H. and Giacomin, A. J.}
}
@article { ISI:000276190900021,
	title = {Structure and gelation mechanism of silk hydrogels},
	journal = {Physical Chemistry Chemical Physics},
	volume = {12},
	number = {15},
	year = {2010},
	month = {FEB},
	pages = {3834-3844},
	publisher = {ROYAL SOC CHEMISTRY},
	address = {THOMAS GRAHAM HOUSE, SCIENCE PARK, MILTON RD, CAMBRIDGE CB4 0WF, CAMBS, ENGLAND},
	abstract = {<p>Silk fibroin was regenerated from cocoons produced by the silkworm Bombyx Mori. Light scattering showed that an aqueous solution of the regenerated silk fibroin (RSF) was made of individual proteins with a weight average molar mass of about 4 x 10(5) g mol(-1) and a hydrodynamic radius of about 10 nm. Gel formation of RSF in acidic solutions was investigated as a function of the pH (2-4), concentration (0.5-10 g L(-1)) and temperature (5-70 degrees C). The structure of the gels was studied using light scattering and confocal laser scanning microscopy. The structure was found to be self-similar from length scales of less than 15 nm up to length scales of about 1 mm, and characterized by a correlation length of a few microns. Gel formation was tracked using turbidity, rheology, light scattering and circular dichroism. Gelation involves the formation of self-similar aggregates with a growth rate that increases exponentially. The protein aggregation is correlated to, and perhaps caused by, the formation of beta-sheets, the fraction of which also increases exponentially with time.</p>},
	issn = {1463-9076},
	doi = {10.1039/b916319k},
	author = {Nagarkar, Shailesh and Nicolai, Taco and Chassenieux, Christophe and Lele, Ashish K.}
}
