Antibiofilm elastin-like polypeptide coatings: functionality, stability, and selectivity
Journal article, 2019

Antimicrobial peptides (AMPS) are currently receiving interest as an alternative to conventional antibiotics to treat biomaterial-associated infection. However, the inherent instability of such peptides often limits their efficacy in intended clinical applications. Covalent immobilization of AMPs to surfaces is one strategy to increase the long-term stability and minimize the toxicity. In this work, an antimicrobial peptide, RRPRPRPRPWWWW-NH2 (RRP9W4N), was used to modify elastin-like polypeptide (ELP) surface coatings containing cell-adhesive peptide domains (RGD) using covalent chemistry. The AMP retained its antibacterial activity against Staphylococcus epidermidis, Staphylococcus aureus, and Pseudomonas aeruginosa when covalently bonded to ELP surfaces. Simultaneously, the AMP functionalization had insignificant effect on the viability, function, and differentiation of human osteosarcoma MG63 cells and human mesenchymal stem cells (hMSCs). Furthermore, stability of the immobilized AMP in human blood serum was investigated, and the results suggested that the AMP preserved its antibacterial activity up to 24 h. Combined, the results show that covalently attached AMPs onto RGD-containing ELP are an excellent candidate as an antimicrobial coating for medical devices.




Antimicrobial peptide

Medical device


Saba Atefyekta

Chalmers, Chemistry and Chemical Engineering, Applied Chemistry, Martin Andersson Group

Maria Pihl

Chalmers, Chemistry and Chemical Engineering, Applied Chemistry, Applied Surface Chemistry

Chris Lindsay

Stanford University

Sarah C. Heilshorn

Stanford University

Martin Andersson

Chalmers, Chemistry and Chemical Engineering, Applied Chemistry, Martin Andersson Group

Acta Biomaterialia

1742-7061 (ISSN)

Vol. 83 245-256

Subject Categories

Bioengineering Equipment

Pharmacology and Toxicology

Biomaterials Science





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