4.8 Article

A bioinspired elastin-based protein for a cytocompatible underwater adhesive

期刊

BIOMATERIALS
卷 124, 期 -, 页码 116-125

出版社

ELSEVIER SCI LTD
DOI: 10.1016/j.biomaterials.2017.01.034

关键词

DOPA; Mussel adhesive proteins; Surgical glue; Surgical adhesive; Biomedical glue; Biomedical adhesive

资金

  1. Purdue School of Chemical Engineering and the College of Engineering
  2. National Science Foundation [DMR-1309787, CHE-0952928]
  3. 3M Nontenured Faculty Award
  4. Purdue Research Foundation
  5. Steven C. Beering Fellowship
  6. Office of Naval Research [N00014-13-1-0327, N00014-13-1-0245]
  7. Division Of Materials Research
  8. Direct For Mathematical & Physical Scien [1309787] Funding Source: National Science Foundation

向作者/读者索取更多资源

The development of adhesives that can be applied and create strong bonds underwater is a significant challenge for materials engineering. When the adhesive is intended for biomedical applications, further criteria, such as biocompatibility, must be met. Current biomedical adhesive technologies do not meet these needs. In response, we designed a bioinspired protein system that shows promise to achieve biocompatible underwater adhesion coupled with environmentally responsive behavior that is smart that is, it can be tuned to suit a specific application. The material, ELY16, is constructed from an elastinlike polypeptide (ELP) that can be produced in high yields from Escherichia coli and can coacervate in response to environmental factors such as temperature, pH, and salinity. To confer wet adhesion, we utilized design principles from marine organisms such as mussels and sandcastle worms. When expressed, ELY16 is rich in tyrosine. Upon modification with the tyrosinase enzyme to form mELY16, the tyrosine residues are converted to 3,4-dihydroxyphenylalanine (DOPA). Both ELY16 and mELY16 exhibit cytocompatibility and significant dry adhesion strength (>2 MPa). Modification with DOPA increases protein adsorption to glass and provides moderate adhesion strength (-240 kPa) in a highly humid environment. Furthermore, this ELP exhibits a tunable phase transition behavior that can be formulated to coacervate in physiological conditions and provides a convenient mechanism for application underwater. Finally, mELY16 possesses significantly higher adhesion strength in dry, humid, and underwater environments compared with a commercially available fibrin sealant To our knowledge, mELY16 provides the strongest bonds of any rationally designed protein when used completely underwater, and its high yields make it more viable for commercial application compared to natural adhesive proteins. In conclusion, this ELP shows great potential to be a new smart underwater adhesive. (C) 2017 Elsevier Ltd. All rights reserved.

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