Antimicrobial peptides (AMPs) are potentially powerful alternatives to conventional 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.

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.

Antibiotic resistance in bacteria, especially Gram-positive bacteria like Staphylococcus aureus, is gaining considerable momentum worldwide and unless checked will pose a global health crisis. With few new antibiotics coming on the market, there is a need for novel antimicrobial materials that target and kill multi-drug-resistant (MDR) Gram-positive pathogens like methicillin-resistant Staphylococcus aureus (MRSA).

The day is rapidly approaching where current antibiotic therapies will no longer be effective due to the development of multi-drug resistant bacteria. Antimicrobial peptides (AMPs) are a promising class of therapeutic agents which have the potential to help address this burgeoning problem. Proline-rich AMPs (PrAMPs) are a sub-class of AMPs, that have multiple modes of action including modulation of the bacterial protein folding chaperone, DnaK. They are highly effective against Gram-negative bacteria and have low toxicity to mammalian cells.

Highlights

· Detailed activity and mechanistic studies of AMPs, including Pardaxin, MSI-78, dermaseptin-PC (DMPC) and Cecropin B, against a panel of Gram-negative and Gram-positive bacteria.

· The most active Pardaxin (1–22) and MSI-78 (4–20) displayed strong membrane activity towards Gram-negative and Gram-positive bacteria.

· Different mechanisms of DMPC (1–19) and Cecropin B (1–21) against Gram-negative and Gram-positive bacteria will guide the rational design of new AMP analogues.

· Molecular dynamics simulation further provided the details of their structure and activity relationship.

Highlights

· AIE scaffold (ENAP) created through a facile catalyst-free Diels-Alder reaction

· Introduce the sulfonyl fluoride group as a hub for further modification

· Utilize ENAPs to develop high-quality latent fingerprint images

· Utilize ENAPs for bioimaging

Antimicrobial peptides (AMPs) are host defense peptides, and unlike conventional antibiotics, they possess potent broad spectrum activities and, induce little or no antimicrobial resistance. They are attractive lead molecules for rational development to improve their therapeutic index.

Crustins are an antimicrobial peptide (AMP) family that plays an important role in innate immunity in crustaceans. It is important to discover new AMPs from natural sources to expand the current database. Here, we identified and characterized a new crustin family member, named AaCrus1, from Amphibalanus amphitrite.