Akademik Veri Yönetim Sistemi
Advances in Protein Chemistry and Structural Biology, Academic Press , ss.115-141, 2026
The emergence of antibiotic-resistant pathogens mostly due to intensive antibiotic use greatly endangers human health. For this reason, it has become necessary to search for new drugs or alternative treatments that are effective on resistant microorganisms. This review examines antimicrobial peptides (AMPs) which are part of the first primitive defense mechanism used by both eukaryotic and prokaryotic cells against many pathogens. AMPs are usually small (up to 50 amino acids), cationic peptides which make them bind to negatively charged cell membranes of pathogens for permeabilization and destruction. AMPs can act on antibiotic-resistant pathogens such as Enterococcus faecium, methicillin-resistant Staphylococcus aureus (MRSA), and Pseudomonas aeruginosa, and they offer unique advantages due to their membrane-active antimicrobial mechanisms that reduce the likelihood of developing resistance. AMPs have high therapeutic potential due to their broad-spectrum activities, and different mechanisms of action compared to traditional antibiotics. However, their practical application is often hampered by their limited activity, host toxicity and poor stability. To overcome these limitations, natural AMP sequences can be improved by protein engineering approaches. Surface display technology is one of the leading high-throughput protein engineering strategies where primary/secondary structures of AMPs can be modified and screened for various improvements. This review focuses on the key properties of antimicrobial peptides, as well as insights on the use of in vitro surface display techniques to develop next-generation AMPs for therapeutic uses.