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Peptides & Biochemicals
Antimicrobial Peptides
A comprehensive guide to naturally occurring peptides targeting bacteria, viruses, fungi, and cancer cells.
Antimicrobial peptides (AMPs) are a highly diverse class of small peptides that play a foundational role in the innate immune system. These naturally occurring peptides, typically between 10 and 60 amino acids long, function directly to kill microbes, help maintain immune system homeostasis, and promote wound healing.
AMPs originate from almost all classes of life, including mammals, plants, amphibians, insects, and microorganisms. They are broadly categorized by their targets: anti-bacterial, anti-viral, anti-fungal, anti-parasitic, and anti-cancer.
Mechanisms of Action
AMPs work in various, often overlapping, ways to destroy pathogens without relying on single-protein targets (which is why they rarely induce resistance):
- Membrane Disruption: Through intense electrostatic interactions, AMPs physically embed into and destabilize microbial cell membranes, creating fatal pores leading to lysis.
- Intracellular Targeting: Some AMPs enter cells through endocytosis or direct penetration, interfering with vital internal processes like protein synthesis, nucleic acid synthesis, and cell division.
- Immune Modulation: They can regulate systemic inflammation, rapidly neutralize microbial toxins, stimulate chemotaxis, and help initiate adaptive immunity.
Due to the rapidly increasing threat of antimicrobial resistance to traditional antibiotics in the medical field, AMPs have become a massive research hotspot for novel therapeutics.
1. Anti-bacterial Peptides
Antibacterial peptides represent the largest class of AMPs. Because they act on multiple generalized structural targets (primarily the bacterial membrane), they offer a highly effective alternative to traditional antibiotics and produce significantly fewer resistant strains. They are proven to be effective against difficult targets including MRSA, Listeria monocytogenes, Enterococcus faecium, Klebsiella pneumoniae, and E. coli.
| AMP Name | Amino Acid Sequence | Target Activity |
|---|---|---|
| AMPR-22 | H-Ile-Arg-Ile-Ile-Leu-Arg-Ala-Gln-Gly-Ala-Leu-Lys-Ile-OH |
Anti-bacterial activity against sepsis causing bacteria |
| OP-145 | 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 |
Broad activity against several MRSA strains |
| BING | H-Ile-Arg-Ile-Ile-Leu-Arg-Ala-Gln-Gly-Ala-Leu-Lys-Ile-OH |
Activity against Gram-positive & Gram-negative bacteria |
| Cys-Pexiganan | 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 |
Activity against Gram-positive & Gram-negative bacteria |
| BLP-3 | 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 |
Potent activity against Neisseria, Pseudomonas aeruginosa, and Staphylococcus aureus |
2. Anti-viral Peptides
Viruses are notoriously difficult to treat because they rapidly mutate and hijack host cell machinery. Anti-viral peptides are uniquely suited to target viral infections because they can inhibit viruses at different independent stages of their cycle: they can prevent viral attachment to the cell membrane, impede internal replication, or physically destroy the viral envelope.
| AMP Name | Amino Acid Sequence | Target Activity |
|---|---|---|
| Urumin | 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 |
Targeted activity against Influenza A viruses |
| P9R | 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), coronaviruses, and rhinovirus |
| Magainin 1* | 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 |
Potent activity against Herpes Simplex Virus 1 & 2 |
| Magainin 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 |
Potent activity against Herpes Simplex Virus 1 & 2 |
| Indolicidin* | H-Ile-Leu-Pro-Trp-Lys-Trp-Pro-Trp-Trp-Pro-Trp-Arg-Arg-NH2 |
Activity against the HIV-1 virus |
* Denotes peptides that also exhibit strong anti-bacterial properties.
3. Anti-fungal Peptides
Anti-fungal peptides inhibit the activity of several common, highly resilient fungi, including Candida albicans, Aspergillus, and various molds. They operate primarily by targeting the distinct architecture of the fungal cell wall and membrane, as well as disrupting intracellular protein and DNA synthesis.
| AMP Name | Amino Acid Sequence | Target Activity |
|---|---|---|
| BAC-2A* | H-Arg-Leu-Ala-Arg-Ile-Val-Val-Ile-Arg-Val-Ala-Arg-NH2 |
Potent activity against Candida albicans |
| Histatin 3* | 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 |
Broad activity against fungi, including C. albicans |
| Histatin 5* | 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 |
Broad activity against fungi, including C. albicans |
| RsAFP2 | 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 C. albicans and other Candida species |
| SMAP 29* | 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 |
Broad anti-fungal activity |
* Denotes peptides that also exhibit strong anti-bacterial properties.
4. Anti-parasitic & Anti-cancer Peptides
Certain AMPs possess unique structural properties allowing them to target eukaryotic cells—such as parasites or human cancer cells—without harming healthy host tissues.
Anti-Parasitic & Anti-Cancer
Melittin
Extracted from the venom of the European honey bee. Proven highly effective against parasites causing leishmaniasis and Chagas disease. It also selectively induces apoptosis in breast cancer cells while leaving non-cancerous cells unharmed.
Anti-Cancer
D-K6L9
A specialized, highly active antimicrobial peptide that directly induces tumor cell necrosis in aggressive prostate and breast cancer models.
5. 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
- 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. doi: 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. doi: 10.1016/j.drup.2023.100954