In our immune system, some components hide like shadows, yet invisibly fight against foreign threats. Among them, Cecropin is an antimicrobial peptide in insects, which was first isolated in Hyalophora cecropia (western hawk moth). These small proteins (31 to 37 amino acids long) have demonstrated their inhibitory effects against both Gram-positive and Gram-negative bacteria and are also increasingly showing potential in the fight against cancer.
Cecropins exert their antibacterial effects by lysing bacterial cell membranes and can inhibit proline uptake, leading to membrane leakage.
The Cecropin family also includes different variants, such as Cecropin A, Cecropin B and Cecropin P1. The common features of these peptides are their structural characteristics and their ability to fight bacteria and cancer cells. Scientific research has shown that Cecropin B is particularly outstanding. It not only effectively inhibits bacteria, but also fights cancer cells. In some cases, it shows higher selectivity, while having little effect on normal cells.
Cecropin's anti-cancer activity is rapid in most cases, with studies showing that cancer cells are affected within an hour of treatment, while normal cells have no significant effect.
For example, Cecropin B, along with other variants, exhibited significant cytotoxicity in a variety of cancer cell lines. Many experimental research reports indicate that Cecropin B is also effective against multidrug-resistant breast cancer and ovarian cancer cells, demonstrating its potential anti-cancer ability.
Not only that, Cecropin A has also been shown to selectively destroy leukemia cells with minimal impact on normal lymphocytes. This selectivity makes Cecropin peptides show great promise in cancer treatment.
Studies have shown that Cecropin can be used to reduce the need for chemotherapy drugs, thereby reducing unnecessary side effects.
However, the application of cecropin in cancer therapy faces challenges, mainly how to effectively deliver these peptides to tumor cells, and repeated administration to maintain sufficient concentrations of cecropin in systemic plasma is also a challenge. To address these issues, scientists have proposed gene therapy that involves introducing the Cecropin gene directly into tumor cells.
Studies have shown that when the Cecropin gene is introduced into human bladder cancer cell lines, the tumorigenicity of the tumor cells is significantly reduced, and some cloned tumor cells even completely lose their tumorigenicity. This finding makes Cecropin even more attractive as a cancer treatment prospect.
Recent studies have also identified new Cecropins from various insect species, and these new peptides may contribute to the development of cancer therapies.
For example, Cecropin from Nephila exhibits unusual properties, especially with a BH3-like motif, which may be associated with pro-apoptosis, further enhancing its anti-cancer ability. .
In addition to its antibacterial and anticancer properties, Cecropin A also showed potential against biofilms, particularly pathogenic Escherichia coli (UPEC) associated with urinary tract infections. Cecropin A's ability to break up bacterial biofilms means it can be used in combination with traditional antibiotics such as nesidoxime to clear infections without causing side effects.
In summary, as defense peptides in nature, the potential of Cecropins in antibacterial and anti-cancer activities cannot be underestimated. As research continues to deepen, these small peptides clearly have innovative possibilities in the prospects of anti-tumor treatment. Can Cecropin become a key to future cancer treatment?