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Protein Engineered Triblock Polymers Composed of Two SADs: Enhanced Mechanical Properties and Binding Abilities

Journal Article · · Biomacromolecules
 [1];  [1];  [1];  [2];  [3];  [1];  [2];  [1];  [1];  [1];  [2];  [4]
  1. New York Univ. (NYU), Brooklyn, NY (United States). Tandon School of Engineering. Chemical and Biomolecular Engineering Dept.
  2. City College of New York, NY (United States). Chemical Engineering Dept.
  3. Brookhaven National Lab. (BNL), Upton, NY (United States). National Synchrotron Light Source II
  4. New York Univ. (NYU), Brooklyn, NY (United States). Tandon School of Engineering. Chemical and Biomolecular Engineering Dept.; SUNY Downstate Medical Center, Brooklyn, NY (United States). Biochemistry Dept.; New York Univ. (NYU), NY (United States). Chemistry Dept. College of Dentistry. Biomaterials Dept.
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. To understand how the two C domains improve small molecule recognition and the mechanical integrity of CEC, we have constructed CL44AECL44A, which bears an impaired CL44A domain that is unstructured as a negative control. The CEC triblock polymer demonstrates increased small molecule binding and ideal elastic behavior for hydrogel formation. The negative control CL44AECL44A does not exhibit binding to small molecule and is inelastic at lower temperatures, affirming the favorable role of C domain and its helical conformation. While both CEC and CL44AECL44A assemble into micelles, CEC is more densely packed with C domains on the surface enabling the development of networks leading to hydrogel formation. Finally, such protein engineered triblock copolymers capable of forming robust hydrogels hold tremendous promise for biomedical applications in drug delivery and tissue engineering.
Research Organization:
Brookhaven National Lab. (BNL), Upton, NY (United States); City College of New York, NY (United States); New York Univ. (NYU), Brooklyn, NY (United States)
Sponsoring Organization:
Army Research Office (ARO) (United States); National Inst. of Health (NIH) (United States); National Science Foundation (NSF) (United States); USDOE Office of Science (SC)
Grant/Contract Number:
SC0012704
OSTI ID:
1464112
Report Number(s):
BNL--207924-2018-JAAM
Journal Information:
Biomacromolecules, Journal Name: Biomacromolecules Journal Issue: 5 Vol. 19; ISSN 1525-7797
Publisher:
American Chemical SocietyCopyright Statement
Country of Publication:
United States
Language:
English

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Cited By (3)

Protein‐Engineered Functional Materials journal April 2019
Elastin-like polypeptides as building motifs toward designing functional nanobiomaterials journal January 2019
Protein biomaterials for theranostic applications journal January 2019

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