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Antimicrobial Peptides
Antimicrobial peptides (AMPs) are a class of small peptides that play an important role in the immune system. These naturally occurring peptides, between 10 and 60 amino acids long, function to kill microbes, help maintain immune system homeostasis, and promote wound healing.
AMPs originate from many types of organisms, including mammals, plants, amphibians, insects, and microorganisms. These peptides can be divided into many classes, including anti-bacterial, anti-viral, anti-fungal, anti-parasitic, and anti-cancer. AMPs have a diversity of applications in the medical and food industries. There are also potential applications in agriculture and animal husbandry.
AMPs work in various ways. Some AMPs act on the cell membranes of microbes. Through the interactions of their physical/chemical properties, AMPs can create holes and destabilize the cell membrane, leading to cell death. Other AMPs enter cells through endocytosis or penetration. These AMPs interfere with different cell processes, including protein synthesis, nucleic acid synthesis, enzyme activity, and cell division. Others can impact microbes on both extracellular and intracellular levels. AMPs that function as immune system modulators have diverse roles. They can help regulate inflammation, neutralize microbial toxins, stimulate chemotaxis, and initiate adaptive immunity.
Due to the increasing threat of antimicrobial resistance in the medical field, AMPs have become a research hotspot.
Anti-bacterial Peptides:
Antibacterial peptides are a large class of AMPs. Because AMPs can act on multiple targets, compared to traditional antibiotics which act on only one, AMPs offer an effective alternative to kill pathogens and produce fewer resistant bacteria. AMPs have been found to target a variety of bacteria, including MRSA, Listeria monocytogenes, Enterococcus faecium, Klebsiella pneumoniae, and E. coli. Below are a few examples of antibacterial peptides and their targets.
AMP | Sequence | Activity |
|---|---|---|
H-Ile-Arg-Ile-Ile-Leu-Arg-Ala-Gln-Gly-Ala-Leu-Lys-Ile-OH | Anti-bacterial activity against sepsis causing bacteria | |
Ac-Ile-Gly-Lys-Glu-Phe-Lys-Arg-Ile-Val-Glu-Arg-Ile-Lys-Arg-Phe-Leu-Arg-Glu-Leu-Val-Arg-Pro-Leu-Arg-NH2 | Anti-bacterial activity against several MRSA strains | |
H-Ile-Arg-Ile-Ile-Leu-Arg-Ala-Gln-Gly-Ala-Leu-Lys-Ile-OH | Antibacterial activity against gram + and – bacteria | |
H-Cys-Gly-Ile-Gly-Lys-Phe-Leu-Lys-Lys-Ala-Lys-Lys-Phe-Gly-Lys-Ala-Phe-Val-Lys-Ile-Leu-Lys-Lys-NH2 | Antibacterial activity against gram + and - bacteria | |
H-Gly-Ile-Gly-Ala-Ala-Ile-Leu-Ser-Ala-Gly-Lys-Ser-Ala-Leu-Lys-Gly-Leu-Ala-Lys-Gly-Leu-Ala-Glu-His-Phe-NH2 | Antibacterial activity against gram + and - bacteria, especially against Neisseria, Pseudomonas aeruginosa, and Staphylococcus aureus |
* Products with asterisks also have anti-bacterial properties.
Anti-viral Peptides:
Viruses can be difficult to treat because they are transmitted quickly through multiple means, rapidly mutate within cells, and are not localized in one area of the body. Anti-viral peptides are being studied as an option to help target viral infections since they can inhibit viruses at different stages of their cycle. For example, they can prevent viruses from attaching to the cell membrane, impede replication, or destroy the viral envelope. Below are a few examples of antiviral peptides and their targets.
AMP | Sequence | Activity |
|---|---|---|
H-Ile-Pro-Leu-Arg-Gly-Ala-Phe-Ile-Asn-Gly-Arg-Trp-Asp-Ser-Gln-Cys-His-Arg-Phe-Ser-Asn-Gly-Ala-Ile-Ala-Cys-Ala-OH | Activity against influenza A viruses | |
H-Asn-Gly-Ala-Ile-Cys-Trp-Gly-Pro-Cys-Pro-Thr-Ala-Phe-Arg-Gln-Ile-Gly-Asn-Cys-Gly-Arg-Phe-Arg-Val-Arg-Cys-Cys-Arg-Ile-Arg-OH | Activity against avian influenza A (H7N9) virus, coronaviruses, and the non-enveloped rhinovirus | |
H-Gly-Ile-Gly-Lys-Phe-Leu-His-Ser-Ala-Gly-Lys-Phe-Gly-Lys-Ala-Phe-Val-Gly-Glu-Ile-Met-Lys-Ser-OH | Activity against herpes simplex virus 1 and 2 | |
H-Gly-Ile-Gly-Lys-Phe-Leu-His-Ser-Ala-Lys-Lys-Phe-Gly-Lys-Ala-Phe-Val-Gly-Glu-Ile-Met-Asn-Ser-OH | Activity against herpes simplex virus 1 and 2 | |
H-Ile-Leu-Pro-Trp-Lys-Trp-Pro-Trp-Trp-Pro-Trp-Arg-Arg-NH2 | Activity against HIV-1 virus |
* Products with asterisks also have anti-bacterial properties.
Anti-fungal Peptides:
Anti-fungal peptides have been found to inhibit the activity of several common fungi, including Candida albicans, Aspergillus, and mold. Anti-fungal peptides can target the cell wall and membrane as well as intracellular processes such as protein and DNA synthesis. Below are a few examples of antifungal peptides and their targets.
AMP | Sequence | Activity |
|---|---|---|
H-Arg-Leu-Ala-Arg-Ile-Val-Val-Ile-Arg-Val-Ala-Arg-NH2 | Activity against Candida albicans | |
H-Asp-Ser-His-Ala-Lys-Arg-His-His-Gly-Tyr-Lys-Arg-Lys-Phe-His-Glu-Lys-His-His-Ser-His-Arg-Gly-Tyr-Arg-Ser-Asn-Tyr-Leu-Tyr-Asp-Asn-OH | Activity against fungi, including Candida albicans | |
H-Asp-Ser-His-Ala-Lys-Arg-His-His-Gly-Tyr-Lys-Arg-Lys-Phe-His-Glu-Lys-His-His-Ser-His-Arg-Gly-Tyr-OH | Activity against fungi, including Candida albicans | |
PyroGlu-Lys-Leu-Cys-Gln-Arg-Pro-Ser-Gly-Thr-Trp-Ser-Gly-Val-Cys-Gly-Asn-Asn-Asn-Ala-Cys-Lys-Asn-Gln-Cys-Ile-Arg-Leu-Glu-Lys-Ala-Arg-His-Gly-Ser-Cys-Asn-Tyr-Val-Phe-Pro-Ala-His-Lys-Cys-Ile-Cys-Tyr-Phe-Pro-Cys-OH | Activity against Candida albicans and other Candida species | |
H-Arg-Gly-Leu-Arg-Arg-Leu-Gly-Arg-Lys-Ile-Ala-His-Gly-Val-Lys-Lys-Tyr-Gly-Pro-Thr-Val-Leu-Arg-Ile-Ile-Arg-Ile-Ala-Gly-OH | Antifungal activity |
* Products with asterisks also have anti-bacterial properties.
Antiparasitic Peptides:
Parasites can also exhibit resistance to drugs. Anti-parasitic peptides have been found to be effective against different parasites, including those that cause malaria, schistosomiasis, chagas disease, and leishmaniasis. Melittin, a peptide extracted from the venom of the European honey bee, has been shown to be effective against the parasites responsible for leishmaniasis and chagas disease.
Anti-cancer Peptides:
Anti-cancer peptides can affect cancer cells in various ways. AMPs can prevent angiogenesis, induce apoptosis, or engage the organism’s immune system to kill cancer cells. In addition to its antiparasitic properties, Melittin can cause apoptosis in breast cancer cells while non-cancerous cells remain unharmed. D-K6L9 is an AMP that causes tumor cell necrosis in prostate cancer and breast cancer tumors.
References
- Fernández de Ullivarri M, Arbulu S, Garcia-Gutierrez E and Cotter PD (2020) Antifungal Peptides as Therapeutic Agents. Front. Cell. Infect. Microbiol. 10:105. doi: 10.3389/fcimb.2020.00105
- Huan Y, Kong Q, Mou H, Yi H. Antimicrobial Peptides: Classification, Design, Application and Research Progress in Multiple Fields. Front Microbiol. 2020 Oct 16;11:582779. doi: 10.3389/fmicb.2020.582779. PMID: 33178164; PMCID: PMC7596191.
- Jabeen M, Biswas P, Islam MT, Paul R. Antiviral Peptides in Antimicrobial Surface Coatings—From Current Techniques to Potential Applications. Viruses. 2023; 15(3):640. https://doi.org/10.3390/v15030640
- Mahlapuu M, Håkansson J, Ringstad L and Björn C (2016) Antimicrobial Peptides: An Emerging Category of Therapeutic Agents. Front. Cell. Infect. Microbiol. 6:194. doi: 10.3389/fcimb.2016.00194
- Xuan J, Feng W, Wang J, Wang R, Zhang B, Bo L, Chen Z, Yang H, Sun L. Antimicrobial peptides for combating drug-resistant bacterial infections, Drug Resistance Updates, Volume 68, 2023, 100954, ISSN 1368-7646, https://doi.org/10.1016/j.drup.2023.100954.