Biological Function of Antimicrobial Peptides on Suppressing Pathogens and Improving Host Immunity

Abstract

The emergence of drug-resistant genes and concerns about food safety caused by the overuse of antibiotics are becoming increasingly prominent. There is an urgent need for effective alternatives to antibiotics in the fields of livestock production and human medicine. Antimicrobial peptides can effectively replace antibiotics to kill pathogens and enhance the immune functions of the host, and pathogens cannot easily produce genes that are resistant to them. The ability of antimicrobial peptides (AMPs) to kill pathogens is associated with their structure and physicochemical properties, such as their conformation, electrical charges, hydrophilicity, and hydrophobicity. AMPs regulate the activity of immunological cells and stimulate the secretion of inflammatory cytokines via the activation of the NF-κB and MAPK signaling pathways. However, there are still some limitations to the application of AMPs in the fields of livestock production and human medicine, including a restricted source base, high costs of purification and expression, and the instability of the intestines of animals and humans. This review summarizes the information on AMPs as effective antibiotic substitutes to improve the immunological functions of the host through suppressing pathogens and regulating inflammatory responses. Potential challenges for the commercial application of AMPs in animal husbandry and human medicine are discussed.

Recent Advances in the Field of Amino Acid-Conjugated Aminoferrocenes—A Personal Perspective

“…Leu 5-16 [33] The potential of antimicrobial peptides in combating pathogens is related to their structure and physicochemical properties, such as conformation, electrical charge, hydrophilicity, and hydrophobicity [90]. Therefore, we performed the synthesis, detailed conformational analysis, and biological evaluation of 12 conjugates of amino-functionalized ferrocene with Phe, Val, and Leu containing hydrophobic branched and bulky side chains [33].…”

Gallium-based metal–organic frameworks loaded with antimicrobial peptides for synergistic killing of drug-resistant bacteria

“…Taking advantage of the potent broad-spectrum antibacterial activity, unique antibacterial mechanisms, and relatively weak induced drug resistance, antimicrobial peptides (AMPs) have become a good candidate to replace antibiotics. 8–11 Nevertheless, some AMPs are limited by their poor stability under physiological conditions, and strong toxicity to eukaryotic cells ( e.g. , inducing hemolysis).…”

“…Taking advantage of the potent broad-spectrum antibacterial activity, unique antibacterial mechanisms, and relatively weak induced drug resistance, antimicrobial peptides (AMPs) have become a good candidate to replace antibiotics. [8][9][10][11] Nevertheless, some AMPs are limited by their poor stability under physiological conditions, and strong toxicity to eukaryotic cells (e.g., inducing hemolysis). 12,13 To overcome these problems, numerous strategies have been developed to improve the stability of AMPs and to attenuate their toxicity to host cells, such as the optimization of their chemical structures and the loading of these peptides by using carriers.…”

New Perspective for Using Antimicrobial and Cell-Penetrating Peptides to Increase Efficacy of Antineoplastic 5-FU in Cancer Cells

“…AMPs are synthetic or natural peptides with short amino acid sequences (10-60 amino acids) with antimicrobial or anticancer activity [12,13]. Most AMPs are cationic and amphipathic molecules produced by prokaryotic and eukaryotic organisms as part of the host's innate immune system [14,15]. Indeed, cationic AMPs (CAMPs) disrupt the membranes of microbial cells by interacting with negatively charged phospholipids, leading to the formation of pores in the microbial membrane, which causes the leakage of cytoplasmic components and cell death [13,16].…”