Antimicrobial Peptides: Interaction With Model and Biological Membranes and Synergism With Chemical Antibiotics

Abstract

Antimicrobial peptides (AMPs) are promising novel antibiotics since they have shown antimicrobial activity against a wide range of bacterial species, including multiresistant bacteria; however, toxicity is the major barrier to convert antimicrobial peptides into active drugs. A profound and proper understanding of the complex interactions between these peptides and biological membranes using biophysical tools and model membranes seems to be a key factor in the race to develop a suitable antimicrobial peptide therapy for clinical use. In the search for such therapy, different combined approaches with conventional antibiotics have been evaluated in recent years and demonstrated to improve the therapeutic potential of AMPs. Some of these approaches have revealed promising additive or synergistic activity between AMPs and chemical antibiotics. This review will give an insight into the possibilities that physicochemical tools can give in the AMPs research and also address the state of the art on the current promising combined therapies between AMPs and conventional antibiotics, which appear to be a plausible future opportunity for AMPs treatment.

Design and characterization of chionodracine-derived antimicrobial peptides with enhanced activity against drug-resistant human pathogens

“…In the last few decades, the number of infections caused by antibiotic-resistant bacteria has increased dramatically, calling for new and more powerful antimicrobial agents (Center for Disease Control, https://www.cdc.gov/). Therefore, AMPs and [56][57][58][59][60][61] In this work, we explored the possibility to improve the potency and selectivity of Cnd designing new analogs. We changed charge and hydrophobic moments of Cnd wild-type to steer their binding preference toward the negatively charged bacterial membranes.…”

Development and Challenges of Antimicrobial Peptides for Therapeutic Applications

“…Gramicidin is small (10 amino acids) and has a net charge of +2, but it contains eight hydrophobic residues and two positively charged lysine residues, which makes it a small cationic hydrophobic peptide. Many studies have proposed that membrane-active AMPs selectively target and disrupt anionic bacterial cell membranes using electrostatic interactions [45][46][47][48][49]. However, daptomycin, a small amphipathic peptide with a neutral net charge, deviates from this pattern.…”

Insect Antimicrobial Peptides, a Mini Review

“…Thus, the microbial membrane is usually considered the primary target of AMPs [ 9 , 10 ]. Moreover, their outstanding membrane disruptive activity makes these peptides ideal candidates for combined therapies with conventional antibiotics [ 11 ]. AMPs can facilitate more antibiotic molecules entering the microorganism cytoplasm, where they can interact with their target ( Figure 1 ).…”