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• W2080788812 startingPage "2488" @default.
• W2080788812 abstract "Due to their biocompatibility, biodegradability, and low immunogenicity, recombinant spider silk proteins have a high potential for a variety of applications when processed into morphologies such as films, capsules, beads, or hydrogels. Here, hydrogels made of the engineered and recombinantly produced spider silk protein eADF4(C16) were analyzed in detail. It has previously been shown that eADF4(C16) nanofibrils self-assemble by a mechanism of nucleation-aggregation, providing the basis of silk hydrogels. We focused on establishing a reproducible gelation process by employing different protein concentrations, chemical crosslinking, and functionalization of eADF4(C16) with fluorescein. Fluorescein strongly influenced assembly as well as the properties of the hydrogels, such as pore sizes and mechanical behavior, possibly due to its interference with packing of silk nanofibrils during hydrogel formation." @default.
• W2080788812 created "2016-06-24" @default.
• W2080788812 creator A5043996285 @default.
• W2080788812 creator A5062671258 @default.
• W2080788812 date "2011-06-07" @default.
• W2080788812 modified "2023-10-16" @default.
• W2080788812 title "Controlled Hydrogel Formation of a Recombinant Spider Silk Protein" @default.
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• W2080788812 doi "https://doi.org/10.1021/bm200154k" @default.
• W2080788812 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/21612299" @default.
• W2080788812 hasPublicationYear "2011" @default.
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