Antimicrobial peptides: mechanism of action Antibacterial peptides (AMPs) represent a critical class of molecules with significant potential as therapeutic agents. This review delves into the multifaceted nature of antibacterial peptides, exploring their structure, diverse mechanisms of action against pathogens, and their emerging roles in addressing the growing threat of antibiotic resistance. As promising alternatives to conventional antibiotics, AMPs offer a unique approach to combating infections, exhibiting broad-spectrum activity and novel modes of action.
Antimicrobial peptides, often referred to as AMPs, are a diverse group of small molecules, typically composed of 6 to 60 amino acid residuesAntimicrobial peptides are potent antibiofilm agentspossessing a promising broad spectrum of activity for the treatment of a variety of infections caused by .... They are naturally produced by multicellular organisms as part of their innate immune defense system, providing protection against a wide array of pathogens, including bacteria, fungi, viruses, and parasites. Their amphipathic nature, characterized by both hydrophobic and hydrophilic regions, is crucial for their interaction with microbial cell membranes.
AMPs can be broadly classified based on their structural features, such as:
* Alpha-helical peptides: These peptides adopt an alpha-helical conformation, often with a distinct separation of charged and hydrophobic residues that facilitates membrane disruption.
* Beta-sheet peptides: Characterized by beta-sheet structures stabilized by disulfide bonds, these peptides can also interact with and permeabilize bacterial membranes.
* Peptides with mixed alpha/beta structures: This category encompasses peptides that exhibit a combination of helical and sheet elements.
* Extended or random coil peptides: Some AMPs do not adopt rigid secondary structures in isolation but can form ordered structures upon interaction with microbial targets.
This structural diversity underpins their varied mechanisms of action and their ability to target different types of microbes.A Review of Antimicrobial Peptides: Its Function, Mode of ...
The primary mechanism by which many antibacterial peptides exert their effects involves disruption of the microbial cell membrane. Their amphipathic properties allow them to insert into the lipid bilayer, leading to pore formation, membrane permeabilization, and ultimately, cell death.Antimicrobial Peptides in Gut Health: A Review Several models describe this interaction, including the barrel-stave, toroidal pore, and carpet models.作者：HK Kang·2017·被引用次数：487—The review focuses on theuniversal trends in the effective design, mechanism, and biological evolution of AMPs. Article PDF. Download to read ...
Beyond membrane disruption, AMPs can also act through intracellular mechanisms. These include:
* Inhibition of essential cellular processes: Some AMPs can translocate across the bacterial membrane and interfere with vital functions such as DNA replication, RNA synthesis, protein synthesis, and enzymatic activity作者：BP Lazzaro·2020·被引用次数：1075—Antimicrobial peptides(AMPs) are small proteins with potentantibacterial, antiviral, and antifungal activity..
* Induction of oxidative stress: Certain AMPs can trigger the generation of reactive oxygen species within microbial cells, leading to cellular damage作者：MD Seo·2012·被引用次数：650—In this review, we focus onsmall peptides, especially those with less than twelve amino acids, and provide an overview of the relationships between their ....
* Modulation of host immune responses: Intriguingly, some AMPs also possess immunomodulatory properties, which can aid in clearing infections by influencing the host's own defenses, reducing inflammation, and promoting tissue repair.
The ability of AMPs to target multiple cellular components and pathways makes it challenging for bacteria to develop resistance.
The unique properties of antibacterial peptides make them highly attractive for a variety of therapeutic applications, particularly in the face of rising antibiotic resistance. Their potential applications include:
* Treatment of bacterial infections: AMPs show potent activity against a broad spectrum of pathogenic bacteria, including multidrug-resistant strains like methicillin-resistant *Staphylococcus aureus* (MRSA) and vancomycin-resistant enterococci (VRE).Harnessing bacterial antimicrobial peptides: a comprehensive ...
* Wound healing: AMPs can promote wound healing by their antimicrobial activity, reducing bacterial load, and by modulating the inflammatory response.
* Antimicrobial coatings and materials: Incorporating AMPs into medical devices, implants, and wound dressings can prevent biofilm formation and reduce the risk of hospital-acquired infections.
* Food preservation: Certain AMPs exhibit good antibacterial effects against foodborne pathogens, offering a natural alternative for food preservation.
* Drug delivery: AMPs are being explored as carriers for delivering other therapeutic agents to specific sites within the body.
Despite their promise, challenges remain in translating AMPs into widely used clinical drugs. These include issues related to their stability, delivery, potential toxicity, and cost-effective production. However, ongoing research into peptide design, chemical modifications, and novel delivery systems, such as nanocarriers, is steadily addressing these limitations.
As the global health crisis of antimicrobial resistance intensifies, the development of novel therapeutic strategies is paramount. Antibacterial peptides, with their distinct mechanisms of action and inherent ability to evade resistance, stand out as a crucial frontier in this battle.作者：M Alzain·2025·被引用次数：10—Thisreviewprovides a comprehensive overview of AMP origins, characteristics, mechanisms, applications, and future prospects in combating ... Continued research into their intricate properties, mechanisms, and diverse applications, coupled with advancements in peptide engineering and clinical development, holds significant promise for ushering in a new era of effective infection control. The exploration of both naturally occurring and synthetically designed peptides, including those with low off-target hemolysis toxicity and excellent plasma stability, will be key to unlocking their full therapeutic potential.
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