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    Home > Biochemistry News > Biotechnology News > Antibiotic "blue" successor - antimicrobial peptides

    Antibiotic "blue" successor - antimicrobial peptides

    • Last Update: 2021-01-22
    • Source: Internet
    • Author: User
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    Perhaps the most important drug in World War II belonged to the antibiotic penicillin, penicillin, but after so many years of development, it has long since faded from our view, more and more antibiotics are springing up, but the widespread and large quantities of antibiotics caused by a very deadly problem (resistance) is gradually highlighted.
    this is a global crisis and challenge that requires global cooperation and comprehensive efforts to design and produce effective antimicrobial agents that limit the spread of drug-resistant pathogens.
    antibacterial peptides are considered to have broad application prospects in the pharmaceutical industry because of their high antibacterial activity, wide antibacterial spectrum, wide range of options, and the fact that the target strains are not susceptible to resistance mutations.
    , a variety of peptide antibiotics are currently being studied in preclinical feasibility studies, of which magainins have entered phase III clinical trials.
    Antibacterial Peptide Introduction Antibacterial Peptide refers to a class of alkaline peptides with antibacterial activity induced in the body, with a molecular weight of about 2000 to 7000, consisting of 20 to 60 amino acid residues.
    of these active peptides have strong alkaline, thermal stability and broad-spectrum antibacterial characteristics.
    antimicrobial peptides can be roughly divided into four categories according to their structure: spiral, flaky, extended and ring-shaped.
    some antimicrobial peptides are made up entirely of a spiral or flake, while others have more complex structures.
    of these extended peptides is the lack of an identifiable structural base sequence.
    However, they contain a large number of specific amino acids, such as arginine, tryptophan, glycine and histamine, and the diversity of their three-dimensional antimicrobial peptide structures is shown in the following illustration: The first evidence of the key role of antimicrobial peptides in insect defence systems was obtained in 1996, when Ho mann and colleagues demonstrated that genetic mechanisms to remove antimicrobial peptide synthesis make fruit flies vulnerable to fungal infections.
    , with the discovery of the important role of antimicrobial peptides in mammalian host defense, the scientific research and clinical application of antimicrobial peptides have been paid more and more attention.
    , almost all multicellular organisms have found and identified antimicrobial peptides.
    current antimicrobial peptide database contains more than 3000 antimicrobial peptides, and this number is expected to increase further in the coming years.
    the most common mechanism of antimicrobial peptides is through their direct activity on bacterial cell membranes.
    in short, antimicrobial peptide binding leads to damage to membrane levels, changes in membrane permeability, and leakage of metabolites, which eventually leads to the death of bacterial cells.
    of antimicrobial peptides helps their ability to interact with bacterial membranes.
    antimicrobial peptides have a net positive charge and are therefore known as cation antimicrobial peptides.
    electrostic interaction between cation antimicrobial peptides and anion bacterial membranes stabilizes the binding of antimicrobial peptides with bacterial membranes.
    , the bacterial membrane is destroyed, causing antibacterial peptides to enter the membrane, usually creating pores.
    advantage of antimicrobial peptides is that they have fixed biological targets for traditional antibiotics.
    addition, a unique feature of many antimicrobial peptides is their multiple mechanisms of action, which together constitute their overall antibacterial activity.
    , for example, human-sourced cathelicidin LL-37 exhibits direct antimicrobial annihilation, immunomodulation, and anti-biofilm activity.
    most common effect of LL-37 is to act on bacterial cell membranes, but also to regulate the anti-inflammatory and anti-inflammatory immune response.
    , LL-37 performs anti-biofilm activity at physiologically relevant concentrations, well below its in-body minimum inhibition concentration (MIC).
    , antimicrobial peptides, such as LL-37, have a mechanism of effect of diversity and dose dependence.
    the therapeutic potential of antimicrobial peptides The ability of antimicrobial peptides to function through a variety of mechanisms and different channels not only increases their antibacterial activity, but also reduces the tendency to develop resistance.
    can greatly reduce the likelihood that bacteria will get multiple mutations at the same time, making antimicrobial peptides have good therapeutic potential for drug resistance.
    In addition, since many antimicrobial peptides act on the cell membrane locations of bacteria, bacteria must completely redesign the structure of their cell membranes to mutate, and multiple mutations may occur over a longer period of time.
    in cancer chemotherapy, it is common to use a combination of drugs with different mechanisms to limit tumor resistance.
    , however, the use of multiple drugs increases the potential side effects and toxicity of chemotherapy.
    , a single antimicrobial peptide drug with multiple complementary mechanisms may have the same antibacterial effect with minimal side effects.
    these excellent properties of antimicrobial peptides also lead to another potential treatment that is combined with antibiotics, namely antimicrobial peptides in the same way as antibiotics, which can significantly reduce or bypass the occurrence of antibiotic resistance.
    , for example, the antimicrobial peptide DP7 combined treatment can be very good to eradicate Staphylococcus auspicillus, E. coli resistance to vancomycin and azithromycin.
    suggests that the toxicity or side effects of a drug can be reduced in clinical relevance when used in low doses.
    antimicrobial peptides not only show synergy with antibiotics, but may also work with components of the immune system.
    there are a lot of natural antimicrobial peptides that work well, there are still a lot of potential modifications that can be used to produce new antimicrobial peptides.
    , for example, peptides are peptide analogs that are resistant to protein hydrolysalization and can therefore extend their half-life for treatment.
    these peptide simulators, the side chain is attached to the nitrogen atom, not to α carbon.
    of the antibacterial peptide magainin has been developed to regulate the composition of aromatic groups and adjust the total charge on molecules.
    also been observed in this magainin simulation, including neutral granulocyte metastases and enhanced macrophage activation.
    future of antimicrobial peptides Global calls for action to develop new antimicrobial compounds to avoid the next antimicrobial crisis.
    large number of antimicrobial peptides in clinical trials, demonstrating their clinical potential.
    as a promising class of antimicrobial compounds, antimicrobial peptides still have a lot of work to do.
    antimicrobial peptides in clinical trials have not been brought to market due to poor design or lack of effectiveness.
    , more research into the interaction between peptide-based antimicrobials and complex human environments will help to assess the true potential of these drugs.
    chemically modifying the structure of antimicrobial peptides is almost infinitely possible.
    determine a common drug group and ideal modifications will enhance the capacity of compounds for clinical trials.
    fact, many compounds in clinical trials are chemically modified to improve their medicinal properties.
    this process, we actively utilize advanced digital libraries and modeling software to further optimize the development of these compounds, resulting in continuous optimization of success and efficacy.
    it must be emphasized that while the design and development of antimicrobial peptides is a far-reaching task, we must not repeat the mistakes of the past and must strive to limit resistance to new antimicrobial compounds.
    although studies have shown a lower propensity for antimicrobial peptides, this phenomenon is an inevitable evolutionary result.
    development of a variety of antimicrobial compounds and antimicrobial mechanisms will help limit the impact of antibiotic resistance.
    addition, when a new antimicrobial is on the market, it will require detailed monitoring and management.
    the use of antimicrobials in non-essential cases, or in occity with antibiotics, will further limit the risk of drug-resistant bacteria.
    : 1.Lemaitre B, Nicolas E, Michaut L, et al. The dorsoventral regulatory gene cassette spätzle/Toll/cactus controls the potent antifungal response in Drosophila adults[J]. Cell, 1996, 86(6): 973-983. 2.Kumar P, Kizhakkedathu J N, Straus S K. Antimicrobial peptides: diversity, mechanism of action and strategies to improve the activity and biocompatibility in vivo[J]. Biomolecules, 2018, 8(1): 4. 3.Bucki R, Leszczyńska K, Namiot A, et al. Cathelicidin LL-37: a multitask antimicrobial peptide[J]. Archivum immunologiae et therapiae experimentalis, 2010, 58(1): 15-25. 4.Marr A K, Gooderham W J, Hancock R E W. Antibacterial peptides for therapeutic use: obstacles and realistic outlook[J]. Current opinion in pharmacology, 2006, 6(5): 468-472. 5.Suzuki N, Hazama S, Iguchi H, et al. Phase II clinical trial of peptide cocktail therapy for patients with advanced pancreatic cancer: VENUS‐PC study[J]. Cancer science, 2017, 108(1): 73-80. 6.Pasupuleti M, Schmidtchen A, Malmsten M. Antimicrobial peptides: key components of the innate immune system[J]. Critical reviews in biotechnology, 2012, 32(2): 143-171.
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