Antimicrobial peptides (AMPs) are short peptides (usually less than 100 amino acids) found in many organisms, including plants, animals, and humans. They are important components of the innate immune system and can target a wide range of pathogens, including bacteria, fungi, and viruses. AMPs are typically cationic and amphipathic, allowing them to interact with and disrupt the membranes of pathogens. They can act through various mechanisms, such as membrane disruption, targeting intracellular components, or interfering with metabolic pathways. AMPs are particularly valuable in combating antibiotic-resistant strains and have potential applications in medicine, agriculture, and food preservation. AMPs are found in various sources, including plants, animals, and humans. Plant AMPs are often cysteine-rich and contain multiple disulfide bridges, providing structural stability. They are divided into several classes, such as thionins, defensins, hevein-like peptides, knottins, α-hairpinins, lipid transfer proteins, snakins, and non-cysteine-rich peptides. These AMPs have diverse functions, including antibacterial, antifungal, and antiviral activities. In animals, AMPs are primarily found in the defensin and cathelicidin families. These peptides are involved in immune defense and can target both Gram-positive and Gram-negative bacteria. In humans, AMPs include LL-37, which is part of the cathelicidin family and has antibacterial and anti-inflammatory properties. Other human AMPs include defensins, cathelicidins, and histatins, which are found in various tissues and have roles in immune defense. AMPs can act through different mechanisms, including membrane disruption, targeting intracellular components, and interfering with metabolic pathways. The most common mechanisms involve membrane disruption, such as forming pores and channels that lead to cell death. Other mechanisms include targeting viral proteins, inhibiting DNA and RNA synthesis, and disrupting cellular processes. Despite their potential, AMPs face challenges such as poor stability, susceptibility to proteolytic degradation, and limited bioavailability. Strategies to improve their stability and activity include chemical modification, cyclization, peptidomimetics, and nanotechnology. These approaches aim to enhance the antimicrobial activity of AMPs while reducing their degradation and improving their therapeutic potential.Antimicrobial peptides (AMPs) are short peptides (usually less than 100 amino acids) found in many organisms, including plants, animals, and humans. They are important components of the innate immune system and can target a wide range of pathogens, including bacteria, fungi, and viruses. AMPs are typically cationic and amphipathic, allowing them to interact with and disrupt the membranes of pathogens. They can act through various mechanisms, such as membrane disruption, targeting intracellular components, or interfering with metabolic pathways. AMPs are particularly valuable in combating antibiotic-resistant strains and have potential applications in medicine, agriculture, and food preservation. AMPs are found in various sources, including plants, animals, and humans. Plant AMPs are often cysteine-rich and contain multiple disulfide bridges, providing structural stability. They are divided into several classes, such as thionins, defensins, hevein-like peptides, knottins, α-hairpinins, lipid transfer proteins, snakins, and non-cysteine-rich peptides. These AMPs have diverse functions, including antibacterial, antifungal, and antiviral activities. In animals, AMPs are primarily found in the defensin and cathelicidin families. These peptides are involved in immune defense and can target both Gram-positive and Gram-negative bacteria. In humans, AMPs include LL-37, which is part of the cathelicidin family and has antibacterial and anti-inflammatory properties. Other human AMPs include defensins, cathelicidins, and histatins, which are found in various tissues and have roles in immune defense. AMPs can act through different mechanisms, including membrane disruption, targeting intracellular components, and interfering with metabolic pathways. The most common mechanisms involve membrane disruption, such as forming pores and channels that lead to cell death. Other mechanisms include targeting viral proteins, inhibiting DNA and RNA synthesis, and disrupting cellular processes. Despite their potential, AMPs face challenges such as poor stability, susceptibility to proteolytic degradation, and limited bioavailability. Strategies to improve their stability and activity include chemical modification, cyclization, peptidomimetics, and nanotechnology. These approaches aim to enhance the antimicrobial activity of AMPs while reducing their degradation and improving their therapeutic potential.