Antibiotic peptide-modified nanostructured titanium surface for enhancing bactericidal property
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The infections associated with titanium-based biomaterials have been one of the most serious postoperative complications in the orthopedic surgery. Great efforts have been made to improve the antimicrobial property of titanium-based biomaterials by virtue of the surface modification strategy. From the biomimetic perspective of vegetation roots anchoring soil, alkali treatment was conducted on metallic titanium to produce a nanoroot-structured surface in the present study; then, antimicrobial peptide was anchored within the nanoroot surface by vacuum extraction and lyophilization. As a result, the obtained antibacterial peptide-leashed titanium surface showed a hierarchical structure combining the designed nanoroot topography and the anchored antibiotic peptide. Furthermore, this modified surface could steadily release for more than 10 h in a time-dependent manner. As a consequence, the elaborate antimicrobial peptide-loaded surface demonstrated a powerful antibacterial and biofilm-resistant capability against two types of Staphylococcus, without significant cytotoxicity. Specifically, Peptide-2 can kill the most planktonic and sessile bacteria for two gram-positive bacteria. Therefore, the integration of antibacterial peptide onto titanium-based implant surface may be a hopeful tool to prevent implant-associated infections in the orthopedic surgery.
This work was supported by the National Natural Science Foundation of China (Grant No. 81401815), the China Postdoctoral Science Foundation (Grant No. 2015M582900) and the Jiangsu Postdoctoral Science Foundation (Grant No. 1501146C).
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Conflict of interest
The authors declare that they have no conflict of interest.
- 44.Li J, Liu X, Wen C (eds) (2015) Surface coating and modification of metallic biomaterials. Woodhead Publishing, SawstonGoogle Scholar
- 70.Garcia JR, Jaumann F, Schulz S et al (2001) Identification of a novel, multifunctional beta-defensin (human beta-defensin 3) with specific antimicrobial activity. Its interaction with plasma membranes of Xenopus oocytes and the induction of macrophage chemoattraction. Cell Tissue Res 306:257–264CrossRefGoogle Scholar
- 71.Chaly YV, Paleolog EM, Kolesnikova TS, Tikhonov II, Petratchenko EV, Voitenok NN (2000) Neutrophil alpha-defensin human neutrophil peptide modulates cytokine production in human monocytes and adhesion molecule expression in endothelial cells. Eur Cytokine Netw 11:257–266Google Scholar