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Insect peptides with antimicrobial effects

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F62690094%3A18470%2F22%3A50019647" target="_blank" >RIV/62690094:18470/22:50019647 - isvavai.cz</a>

  • Result on the web

    <a href="http://dx.doi.org/10.1016/B978-0-323-85682-9.00015-5" target="_blank" >http://dx.doi.org/10.1016/B978-0-323-85682-9.00015-5</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1016/B978-0-323-85682-9.00015-5" target="_blank" >10.1016/B978-0-323-85682-9.00015-5</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Insect peptides with antimicrobial effects

  • Original language description

    In prokaryotes and eukaryotes, antimicrobial peptides (AMPs) are versatile innate defensive components. AMPs are usually 1250 amino acids (AA) long and are classified into various categories based on AA substitutions, structure, and composition. More than 50% of the total AA consolidate the hydrophobic region of AMPs. AMPs in eukaryotes are produced ribosomally and contribute to the innate immunity of the organism. In contrast, the fungal and bacterial AMPs differ from the former to be synthesized nonribosomally. AMPs are known to possess an array of anticancer activities, antiviral, antifungal, and antibacterial, among others, which make them a suitable candidate as a prophylactic and therapeutic agent. AMP-derived drugs are often employed to treat wound and skin infections in the form of topical preparations. AMPs have an advantage over conventional antibiotics as they are not as susceptible to developing resistance in bacteria as antibiotics. Therefore, they can act as an alternative to antibiotics in the period of antibiotic resistance. AMPs are known to kill a range of pathogens owing to their ability to disintegrate cell membranes. Therefore, the search for AMPs is often directed toward those with the potential to disrupt microbial membranes. Membrane disrupting property of AMPs outstand them as perfect candidates to be employed in combination therapies, especially with traditional antibiotics as AMPs aid in the facilitation of antibiotic molecules into the cell by disrupting the cell membrane, thus allowing the antibiotic to act on its target. It is well versed in the literature that insects are impervious to attack by pathogenic microorganisms. They are known to synthesize a variety of peptides and proteins as a defensive action against bacterial infections. They either directly kill pathogenic microbes and viruses or trigger the immune system to impede them. These defensive proteins and peptides are produced by innate immune cells such as hemocytes. AMPs are involved in multiple defensive responses such as neutralizing and binding to endotoxins, killing pathogenic microbes, and controlling immune responses during infection. The production of AMPs induces a transient humoral immune response marked by increased levels of AMPs in the hemolymph, which tend to last longer than the initial cellular responses, thus acting as back-up for persistent microbial infections. With further exploration, AMPs are involved in modulating endosymbionts apart from their defensive roles. Despite the ubiquity of AMPs amid eukaryotic organisms, they have only been extensively investigated in insects.

  • Czech name

  • Czech description

Classification

  • Type

    C - Chapter in a specialist book

  • CEP classification

  • OECD FORD branch

    10608 - Biochemistry and molecular biology

Result continuities

  • Project

  • Continuities

    I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Others

  • Publication year

    2022

  • Confidentiality

    S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Data specific for result type

  • Book/collection name

    Antimicrobial Peptides: Challenges and Future Perspectives

  • ISBN

    978-0-323-85682-9

  • Number of pages of the result

    22

  • Pages from-to

    117-138

  • Number of pages of the book

    346

  • Publisher name

    Academic Press

  • Place of publication

    New York

  • UT code for WoS chapter