Abstract
Herein, a synthetic polymer proteomimetic is described that reconstitutes the key structural elements and function of mussel adhesive protein. The proteomimetic was prepared via graft-through ring-opening metathesis polymerization of a norbornenyl-peptide monomer. The peptide was derived from the natural underwater glue produced by marine mussels that is composed of a highly repetitive 10 amino acid tandem repeat sequence. The hypothesis was that recapitulation of the repeating unit in this manner would provide a facile route to a nature-inspired adhesive. To this end, the material, in which the arrangement of peptide units was as side chains on a brush polymer rather than in a linear fashion as in the natural protein, was examined and compared to the native protein. Mechanical measurements of adhesion forces between solid surfaces revealed improved adhesion properties over the natural protein, making this strategy attractive for diverse applications. One such application is demonstrated, using the polymers as a surface adhesive for the immobilization of live cells.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 4383-4392 |
| Number of pages | 10 |
| Journal | Journal of the American Chemical Society |
| Volume | 144 |
| Issue number | 10 |
| DOIs | |
| State | Published - Mar 16 2022 |
Funding
The authors would like to thank the members of the Gianneschi Lab for all the insightful discussions and support, Dr. Christopher J. Forman for assistance with graphics, and Dr. Matthew P. Thompson for assistance with peptide synthesis. The authors thank the National Science Foundation, Division of Materials Research (award no. 2004899), for support with materials synthesis and methodology development. Y. Chen acknowledges support from the MRSEC at Northwestern University under NSF (award no. DMR-1720139). This work made use of: (1) The IMSERC NMR and MS facilities at Northwestern University, which have received support from the Soft and Hybrid Nanotechnology Experimental (SHyNE) Resource (NSF ECCS-2025633), and Northwestern University; (2) The Biological Imaging Facility at Northwestern University (RRID: SCR_017767); (3) The SPID facility of Northwestern University’s NUANCE Center, which has received support from the SHyNE Resource (NSF ECCS-2025633), the IIN, and Northwestern University’s MRSEC program (NSF DMR-1720139); and (4) The Keck Biophysics Facility, a shared resource of the Robert H. Lurie Comprehensive Cancer Center of Northwestern University supported in part by the NCI Cancer Center Support grant #P30 CA060553. We thank the Air Force Office of Scientific Research for prior support for the purchase of the AFM equipment used in these studies.
ASJC Scopus subject areas
- General Chemistry
- Biochemistry
- Catalysis
- Colloid and Surface Chemistry
