Protein Engineered Triblock Polymers Composed of Two SADs: Enhanced Mechanical Properties and Binding Abilities
Journal Article
·
· Biomacromolecules
- New York Univ. (NYU), Brooklyn, NY (United States). Tandon School of Engineering. Chemical and Biomolecular Engineering Dept.
- City College of New York, NY (United States). Chemical Engineering Dept.
- Brookhaven National Lab. (BNL), Upton, NY (United States). National Synchrotron Light Source II
- 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
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 |
Similar Records
Controlling Drug Absorption, Release, and Erosion of Photopatterned Protein Engineered Hydrogels
Structure, Morphology, and Rheology of Polyelectrolyte Complex Hydrogels Formed by Self-Assembly of Oppositely Charged Triblock Polyelectrolytes
Mercury-induced crystallization and SAD phasing of the human Fe65-PTB1 domain
Journal Article
·
Mon Jul 27 20:00:00 EDT 2020
· Biomacromolecules
·
OSTI ID:1679965
Structure, Morphology, and Rheology of Polyelectrolyte Complex Hydrogels Formed by Self-Assembly of Oppositely Charged Triblock Polyelectrolytes
Journal Article
·
Tue Jul 28 00:00:00 EDT 2020
· Macromolecules
·
OSTI ID:1768848
Mercury-induced crystallization and SAD phasing of the human Fe65-PTB1 domain
Journal Article
·
Thu May 01 00:00:00 EDT 2008
· Acta Crystallographica. Section F
·
OSTI ID:22360561