Comparison of the structure and function of a chimeric peptide modified titanium surface. Issue 45 (21st August 2019)

• Record Type: Journal Article
• Authors: Gong, Lei; Geng, Hongjuan; Zhang, Xi; Gao, Ping
• Is Part Of: RSC advances. Volume 9:Issue 45(2019)
• Page Start: 26276
• Page End: 26282
• Publication Date: 2019-08-21
• Subjects: Chemistry -- Periodicals; 540.5
• DOI: 10.1039/c9ra05127a
• Languages: English
• ISSNs: 2046-2069

Abstract

Abstract : The antimicrobial activity of Tyr structure in hBD3-3 is stronger than that of the α-helix structure in multifunctional chimeric peptides. Rigid connections avoid functional domain changes. Endogenous peptide fragments on a Ti surface could reduce peri-implant diseases. Abstract : Peri-implantitis is a plaque-initiating infectious disease that can be prevented by interfering with the initial bacterial attachment. At present, surface modification of implants using antimicrobial peptides can interfere with the adhesion of streptococci. In this study, the structure and function of chimeric peptides were compared to get a strategy to modify a Ti surface. Compared to the antimicrobial activity with a fragment of hBD-3, the bifunctional and multifunctional chimeric peptides retain their antimicrobial function. All peptides showed antimicrobial activity against streptococcus in biofilm and planktonic conditions. The results demonstrate significant improvement in reducing bacterial colonization onto titanium surfaces. According to the results of structure analysis, the antimicrobial activity of tyrosine in hBD3-3 was stronger than that of the alpha helix in bifunctional or multifunctional chimeric peptides. Rigid connections were proved to avoid functional domain changes due to the interaction of charges. These results indicated that the endogenous peptide fragments modifying the Ti surface could provide an environmentally friendly approach to reduce or prevent the occurrence of peri-implant diseases.