title: Silk Fibroin-Sophorolipid Gelation: Deciphering the Underlying Mechanism.
abstract: 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.
authors.forename: Parul
authors.initials: P
authors.lastname: Dubey
authors.affiliation: Solid State Physics Division, Bhabha Atomic Research Centre , Mumbai, India.
authors.forename: Sugam
authors.initials: S
authors.lastname: Kumar
authors.affiliation: Solid State Physics Division, Bhabha Atomic Research Centre , Mumbai, India.
authors.forename: Vinod K
authors.initials: VK
authors.lastname: Aswal
authors.forename: Sapna
authors.initials: S
authors.lastname: Ravindranathan
authors.forename: Pattuparambil R
authors.initials: PR
authors.lastname: Rajamohanan
authors.forename: Asmita
authors.initials: A
authors.lastname: Prabhune
authors.forename: Anuya
authors.initials: A
authors.lastname: Nisal
mesh_terms: D000818:Animals; D001672:Biocompatible Materials / Q000737:chemistry; D012831:Bombyx / Q000737:chemistry; D005349:Fibroins / Q000737:chemistry* / Q000648:ultrastructure; D020100:Hydrogels / Q000737:chemistry*; D009682:Magnetic Resonance Spectroscopy; D008823:Micelles; D012212:Rheology; D047011:Silk / Q000737:chemistry* / Q000648:ultrastructure
chemical_list: D001672:Biocompatible Materials; D020100:Hydrogels; D008823:Micelles; D047011:Silk; D005349:Fibroins