The overview of antimicrobial peptide-coated implants against oral bacterial infections

Dental implants are the most common therapeutic approach for resolving tooth loss and damage.Despite technical advances in treatment,implant failure rates can be as high as 23%with the major cause of peri-implantitis:a multi-species bacterial infection.With an annual growth rate in implant placements of 8.78%per annum,implant failure caused by bacterial infection is a significant oral and general health issue.The rise in antibiotic resistance in oral bacteria further adds pressure to implant failure;thus,there is a need for adjunctive therapy to improve implant outcomes.Due to the broad spectrum of activity and a low risk of inducing bacterial resistance,peptide antibiotics are emerging as a promising implant coating material to reduce/prevent peri-implantitis and improve dental implant success rates.In this review,we summarised the current strategies of coating antimicrobial peptides(AMPs)onto dental implant material surfaces with multi-functional properties to enhance osteoblast growth and prevent bacterial infections.This review compared the recent reported literature on dental implant coating with AMPs,which will provide an overview of the current dental implant coating strategies using AMPs and insights for future clinical applications.

The effect of tailing lipidation on the bioactivity of antimicrobial peptides and their aggregation tendency Special Issue:Emerging Investigators

Antimicrobial peptides(AMPs)are potentially powerful alternatives to conven-tional antibiotics in combating multidrug resistance,given their broad spectrum of activity.They mainly interact with cell membranes through surface electrostatic potentials and the formation of secondary structures,resulting in permeability and destruction of target microorganism membranes.Our earlier work showed that two leading AMPs,MSI-78(4–20)and pardaxin(1–22),had potent antimicrobial activ-ity against a range of bacteria.It is known that the attachment of moderate-length lipid carbon chains to cationic peptides can further improve the functionality of these peptides through enhanced interactions with the membrane lipid bilayer,inducing membrane curvature,destabilization,and potential leakage.Thus,in this work,we aimed to investigate the antimicrobial activity,oligomerization propensity,and lipid-membrane binding interactions of a range of N-terminal lipidated analogs of MSI-78(4–20)and pardaxin(1–22).Molecular modeling results suggest that aggregation of the N-lipidated AMPs may impart greater structural stability to the peptides in solu-tion and a greater depth of lipid bilayer insertion for the N-lipidated AMPs over the parental peptide.Our experimental and computationalfindings provide insights into how N-terminal lipidation of AMPs may alter their conformations,with subsequent effects on their functional properties in regard to their self-aggregation behavior,membrane interactions,and antimicrobial activity.