of Health (NIH) (United States) OSTI Identifier: 1464112 Report Number(s): BNL-207924-2018-JAAM Journal ID: ISSN 1525-7797 Grant/Contract Number: SC0012704 W911NF-15-1-0304 DMR-14200407 DGE-0741714 R25GM056833-16 Resource Type: Accepted Manuscript Journal Name: Biomacromolecules Additional Journal Information: Journal Volume: 19 Journal Issue: 5 Journal ID: ISSN 1525-7797 Publisher: American Chemical Society Country of Publication: United States Language: English Subject: 59 BASIC BIOLOGICAL = ,Ī protein-engineered triblock copolymer hydrogel composed of two self-assembling domains (SADs) has been fabricated by a photoactivatable diazirine group followed by ultraviolet (UV)-mediated crosslinking. (NYU), Brooklyn, NY (United States) City College of New York, NY (United States) Sponsoring Org.: USDOE Office of Science (SC) US Army Research Office (ARO) National Science Foundation (NSF) National Inst. (BNL), Upton, NY (United States) New York Univ. Publication Date: Thu Mar 15 00:00: Research Org.: Brookhaven National Lab. SUNY Downstate Medical Center, Brooklyn, NY (United States). Chemical and Biomolecular Engineering Dept. City College of New York, NY (United States).Finally, such protein engineered triblock copolymers capable of forming robust hydrogels hold tremendous promise for biomedical applications in drug delivery and tissue engineering. While both CEC and C L44AEC L44A assemble into micelles, CEC is more densely packed with C domains on the surface enabling the development of networks leading to hydrogel formation. The negative control C L44AEC L44A does not exhibit binding to small molecule and is inelastic at lower temperatures, affirming the favorable role of C domain and its helical conformation.
The CEC triblock polymer demonstrates increased small molecule binding and ideal elastic behavior for hydrogel formation. To understand how the two C domains improve small molecule recognition and the mechanical integrity of CEC, we have constructed C L44AEC L44A, which bears an impaired C L44A domain that is unstructured as a negative control. In this paper, recombinant methods have been used to engineer artificial protein triblock polymers composed of two different self-assembling domains (SADs) bearing one elastin (E) flanked by two cartilage oligomeric matrix protein coiled-coil (C) domains to generate CEC.
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