<?xml version="1.0" encoding="UTF-8"?><xml><records><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>47</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Nagarkara, Shailesh</style></author><author><style face="normal" font="default" size="100%">Lele, Ashish K.</style></author><author><style face="normal" font="default" size="100%">Chassenieux, Christophe</style></author><author><style face="normal" font="default" size="100%">Nicolai, Taco</style></author><author><style face="normal" font="default" size="100%">Durand, Dominique</style></author></authors><secondary-authors><author><style face="normal" font="default" size="100%">Co, A.</style></author><author><style face="normal" font="default" size="100%">Leal, L. G.</style></author><author><style face="normal" font="default" size="100%">Colby, R. H.</style></author><author><style face="normal" font="default" size="100%">Giacomin, A. J.</style></author></secondary-authors></contributors><titles><title><style face="normal" font="default" size="100%">Gelation of regenerated fibroin solution</style></title><secondary-title><style face="normal" font="default" size="100%">15th International Congress on Rheology/80th Annual Meeting of the Society-of-Rheology</style></secondary-title><tertiary-title><style face="normal" font="default" size="100%">AIP CONFERENCE PROCEEDINGS</style></tertiary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">dynamic light scattering</style></keyword><keyword><style  face="normal" font="default" size="100%">Rheology</style></keyword><keyword><style  face="normal" font="default" size="100%">silk fibroin gel</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2008</style></year><pub-dates><date><style  face="normal" font="default" size="100%">AUG</style></date></pub-dates></dates><publisher><style face="normal" font="default" size="100%">Amer Inst Physics, 2 Huntington Quadrangle, STE 1NO1, Melville, NY 11747-4501 USA</style></publisher><pub-location><style face="normal" font="default" size="100%">Monterey, CA.</style></pub-location><volume><style face="normal" font="default" size="100%">1027</style></volume><pages><style face="normal" font="default" size="100%">573-575</style></pages><isbn><style face="normal" font="default" size="100%">978-0-7354-0549-3</style></isbn><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;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.&lt;/p&gt;</style></abstract><notes><style face="normal" font="default" size="100%">15th International Congress on Rheology/80th Annual Meeting of the Society-of-Rheology, Monterey, CA, AUG 03-08, 2008</style></notes></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Nagarkar, Shailesh</style></author><author><style face="normal" font="default" size="100%">Nicolai, Taco</style></author><author><style face="normal" font="default" size="100%">Chassenieux, Christophe</style></author><author><style face="normal" font="default" size="100%">Lele, Ashish K.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Structure and gelation mechanism of silk hydrogels</style></title><secondary-title><style face="normal" font="default" size="100%">Physical Chemistry Chemical Physics</style></secondary-title></titles><dates><year><style  face="normal" font="default" size="100%">2010</style></year><pub-dates><date><style  face="normal" font="default" size="100%">FEB</style></date></pub-dates></dates><number><style face="normal" font="default" size="100%">15</style></number><publisher><style face="normal" font="default" size="100%">ROYAL SOC CHEMISTRY</style></publisher><pub-location><style face="normal" font="default" size="100%">THOMAS GRAHAM HOUSE, SCIENCE PARK, MILTON RD, CAMBRIDGE CB4 0WF, CAMBS, ENGLAND</style></pub-location><volume><style face="normal" font="default" size="100%">12</style></volume><pages><style face="normal" font="default" size="100%">3834-3844</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;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.&lt;/p&gt;</style></abstract><issue><style face="normal" font="default" size="100%">15</style></issue><custom3><style face="normal" font="default" size="100%">Foreign</style></custom3><custom4><style face="normal" font="default" size="100%">3.453</style></custom4></record></records></xml>