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Discovery of Animal Antimicrobial Peptides

There is an urgent need to develop new antimicrobial drugs in order to overcome the increasing resistance of pathogens to existing antibiotics. Antimicrobial peptides (AMPs) are an important component of innate immunity in all animal species. These peptides have a wide range of activity against resistant strains of bacteria. Therefore, animal AMPs are an ideal potential source of novel antimicrobial drugs. Ace Therapeutics provides AMP drug discovery services for antibiotic-resistant pathogens, developing and executing AMP discovery processes to discover AMPs suitable for drug development.

Discovery of AMPs from Animals

Naturally occurring animal antibiotics are an obvious starting point for research. The field of AMP research has gained momentum with the discovery of examples in different species. Examples include asparagine from insects, clawfoot peptides from amphibians and defensins from mammals, to name a few. Since then, a large number of AMPs have been discovered in the animal life community. The diversity of these peptides, which are integral to the innate defense mechanisms of animals, also makes them a rich source for the discovery of drug candidates.

3D structures of defensin from mammals.Fig. 1 3D structures of defensin from mammals. (Koehbach J and Craik D J, 2019)

Our Development Services for AMPs from Animals

Past studies have shown that amphibians have the most abundant AMP diversity known. In vertebrates, AMPs can directly kill microorganisms and play an immunomodulatory role in the infection process. Based on the abundance of AMPs in animals, we can provide development services to isolate and characterize AMPs that can be used against superbug infections from different tissues such as immune cells, body secretions and epithelial tissues of different species such as amphibians, marine and terrestrial animals.

For different animal species

AMPs have been found in virtually all classes of life, from arthropods, amphibians and reptiles to mammals. Therefore, for certain antibiotic-resistant bacteria, we can help you select certain target species that may have potential or screen extensively, including terrestrial mammals, marine organisms, amphibians, insects, animal venom, etc., which are common and important sources of novel antibacterial drugs.

For different structure types

Structurally, animal AMPs can be classified into major groups: β-folded peptides, α-helical peptides, and extended peptides. They may serve as promising candidates for antimicrobial therapy. We can provide research, design and synthesis of peptides with different structures against important human pathogens. We use these peptides as templates or precursor molecules for the development of therapies against drug-resistant bacteria.

For different active

Understanding the mechanism of action of AMP is critical to unlocking its full potential as a next-generation antibiotic. We can conduct extensive studies to uncover the mechanism of action of AMPs. Depending on their MOA, you can choose between AMPs that work through a membrane-disrupting mechanism and those that do not. Ultimately you can achieve broad-spectrum activity, low incidence of bacterial resistance and specific modes of action involving cytoplasmic membrane pore formation.

Our Goals

We are committed to the discovery and design of novel antimicrobial peptides that offer significant advantages over empirical antibiotics against superbugs.

  • Low propensity for resistance selection
  • Rapid killing ability
  • Versatile activity

Please contact us to help you tap into the vast potential of animal AMPs against superbugs.

References

  1. Koehbach J and Craik D J. The vast structural diversity of antimicrobial peptides. Trends in pharmacological sciences, 2019, 40(7): 517-528.
  2. Mwangi J, et al. Antimicrobial peptides: new hope in the war against multidrug resistance. Zool Res, 2019; 40(6): 488-505.
All of our services are intended for preclinical research use only and cannot be used to diagnose, treat or manage patients.
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