Cecropin A–melittin mutant with improved proteolytic stability and enhanced antimicrobial activity against bacteria and fungi associated with gastroenteritis in vitro

Cecropin A-melittin mutant is a potential therapeutic agent in treating bacterial gastroenteritis

“…This suggests CAM-W having a potential in serving as an alternative to conventional antibiotics against bacterial gastroenteritis. In this work, CAM-W displayed an antibacterial activity with a MIC of 0.3 ± 0.10 mg/L toward streptomycin-resistant STEC O157:H7 strain, which is consistent with the MICs ranged from 0.3 to 1.0 mg/L against Gram-negative bacteria reported in the literature [6]. Meanwhile, IC 50 of more than 300 mg/L towards human colorectal adenocarcinoma cell line HT-29 indicates CAM-W having a low cytotoxicity [13].…”

“…CAM-W demonstrates a moderate cytotoxicity (IC 50 > 300 mg/L) in an erythrocyte viability test, a potent antimicrobial activity and also overcomes several challenges under various conditions, involving specific temperatures (20, 30, 40, 50, 60, 70, 80, and 90 C), pH values (2.0, 3.0, 4.0, 5.0, 6.0, 7.0, 8.0, and 9.0), and proteases (trypsin, pepsin, human neutrophil elastase, Pseudomonas aeruginosa elastase, and Staphylococcus aureus V8 protease) [6]. This suggests CAM-W having a potential in serving as an alternative to conventional antibiotics against bacterial gastroenteritis.…”

“…Compared with its parent peptide CAM, CAM-W displays a more potent antimicrobial activity against a wide range of important clinical bacterial and fungal pathogens in vitro, such as Escherichia coli and Aspergillus flavus, and also shows an improved proteolytic stability under a series of proteases including trypsin, pepsin and Staphylococcusaureus V8 protease, which is commonly present in the gastrointestinal tract [6]. In addition, the pH range in the gastrointestinal tract appears to be suitable for the function of CAM-W [6]. Thus, it is suggested that CAM-W has potential as a therapeutic agent in treating bacterial gastroenteritis.…”

“…The use of antimicrobial peptides (AMPs) offers a potential chemotherapeutic strategy to target drug-resistant bacterial pathogens [2][3][4][5]. A fourtryptophan-substitution mutant (KWKLWKKIEKWGQ GIGAVLKWLTTWL-NH 2 ; CAM-W) [6] from cecropin A-melittin (KWKLFKKIEKVGQGIGAVLKVLTTGL-NH 2 ; CAM) [7] has recently been developed through the replacement of specific amino acid residues by four tryptophans (W). Compared with its parent peptide CAM, CAM-W displays a more potent antimicrobial activity against a wide range of important clinical bacterial and fungal pathogens in vitro, such as Escherichia coli and Aspergillus flavus, and also shows an improved proteolytic stability under a series of proteases including trypsin, pepsin and Staphylococcusaureus V8 protease, which is commonly present in the gastrointestinal tract [6].…”

Novel chimeric peptide with enhanced cell specificity and anti-inflammatory activity

“…In particular, a hybrid undecapeptide from cecropin A and melittin possess potent antimicrobial activity while displaying low cytotoxicity [37]. An improved version of this hybrid peptide has been developed with retro and retroenantio analogs [38,39].…”