Classification of Antimicrobial Peptides

Antimicrobial Peptides (AMPs) A class of small peptides which are widely found in nature, they play an important role in the innate immune system. More than 2,600 antimicrobial proteins have been identified so far. They are found in many species, including bacteria, viruses, fungi and fish.

Antimicrobial Peptides

  • Microorganisms-Derived Antimicrobial Peptides

Microorganisms-derived antimicrobial peptides are classified into two types: antimicrobial peptides derived from bacterial and antimicrobial peptides derived from viral. Antibacterial peptides that are derived from bacteria are also known as bacteriocins. Bacteriocins is a type peptide or precursor to peptide molecules that have bactericidal biological activities. They are created by bacteria through the metabolism of protein. These peptides are usually all cationic amino acids chains that are either hydrophobic, or amphiphilic. Biochemical properties allow us to classify bacteriocins into three groups: class I, class II, and class III. Type I bacteriocins can also be called thioether antibiotics. They have a molecular weight of less than 5ku, and a range of amino acid from 19 to 38. They are resistant to heat and have good mucosal activity. They contain rare thioether amino acid structures, including Lanthionine or b-methyllanthione. The class II bacteriocins, also known as lactic acid bacteriacins, are antibacterial peptides that have been discovered in recent years. They can be used to preserve food due to their chemical, biological and physical properties. Class II bacteriocins are slightly less molecular in mass than class I (4-6 ku). Class III bacteriocins, which are produced by bacterial proprotein translocases and have a higher molecular weight than 30 ku and excellent heat resistance, are secreted. Another type of antibacterial peptides is derived from viruses, which can be found in very few types. Among these lentiviral cytolytic peptides (LLPs) are encoded by C-terminal sequences of the human defect virus Type 1 (HIV-1) transmembrane proteins. They have toxic effects on cells and microorganisms. LLPs contain high arginine but no Lysine. In most cases, microorganisms-derived antimicrobial peptides exist in a cyclic structure.

  • Plant-Derived Antimicrobial Peptides

Plant-derived antibacterial propeptides are active against plant pathogens as well as bacterial pathogens that can infect humans. They act as a barrier to plant defense systems and are considered important antibiotic peptides. The most common plant-derived antibacterial proteins are thionin and defensins. Lipid transfer proteins, cells penetrating Peptides, and ecdysone. These peptides share similar properties, including a positive charge and disulfide bond. The target sites are located all within the cell membrane.

  • Insect-Derived Antimicrobial Peptides

With more than 1,000,000 species, insects are among the most common creatures in the natural world. They are adaptable and have developed defense mechanisms. When insects are exposed to the environment, antimicrobial peptides can be produced by the hemolymph and other parts of the body. They are an integral part of the insect’s immune system. The insect’s fat body secretes antibacterial peptides that inhibit various pathogens. There are approximately 200 types of antibacterial proteins that have been isolated from insects. These peptides can be divided into five types based on their antibacterial mechanism or amino acid sequence: Cecropin s Lysozyme defensins , lysozyme and defensins proline rich peptides.

  • Amphibian-Derived Antimicrobial Peptides

Amphibians have exposed skin, high humidity, and a respiratory function. This morphological characteristic and physiological characteristic means that amphibians can only survive in humid environments, which makes it an ideal environment for pathogenic microorganisms to thrive. Amphibians evolved a defense system to combat pathogenic microorganisms in order to adapt to diverse environments and exploit them. When amphibians are subject to stress, trauma, adrenaline or other factors, antibacterial peptides play a crucial role in their immune defense mechanism. The antimicrobial protein gene has been subject to multiple duplications and mutations over the course of long-term evolution. This has resulted in many structures and a variety of antimicrobial proteins. Amphibian skin secretions contain approximately 1,400 antimicrobial proteins. Different sources of antimicrobial bioactive molecules have different secretions. According to their structural characteristics, amphibian-derived antimicrobial proteins can be divided into two groups: cyclic antimicrobial protein peptides that contain intramolecular disulfide bond and linear antimicrobial propeptides with an a-helical configuration.

  • Mammalian Antimicrobial Peptides

Antimicrobial peptides for mammals have no harmful effect on normal animals, but only a lethal effect upon exogenous bacteria. Mammalian antimicrobial proteins are found primarily in mucosal epithelial cell and neutrophils, as well as skin. They include surfactant anionic antimicrobial propeptides in respiratory tract and epithelial tissue defensins. Together, these antimicrobial peptides are the first line of defense for the body. The main categories of mammalian antimicrobial proteins are defensins or cathelicidins. The largest class of antimicrobial proteins is the most widely studied, and they are called defensins. Mammalian defensesins can be divided into two groups: a-defensins or b-defensins.

  • Marine Antimicrobial Peptides

The ocean is home to life’s origins and provides a vast habitat for animals. The ocean is home to approximately half of all the creatures on the planet. This vast biobank is rich in active antibacterial substances. There have been many studies that show that antibacterial peptides are produced by a variety marine organisms. The majority of these antibacterial substances were discovered in research on marine animals. Fishes are most likely to secrete antimicrobial proteins among marine vertebrates. Because of their body structure, antimicrobial proteins are mostly secreted into the mucus layers of marine fish. This acts as the first barrier to the nonspecific immune system from killing pathogenic bacteria before they enter the organism. The characteristics of marine biological antimicrobial proteins are fast synthesis, rapid diffusion, and flexibility. They have a function that is beyond that of any other immune system. Invertebrate marines include molluscs and crustaceans. They rely mainly on the innate immune system of humoral immunity as well as cellular defense systems. Antimicrobial Peptides is an important component of the innate immunity defense system. It can quickly respond to pathogenic microorganisms in real-time.

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