Production Optimization and In Vitro Evaluation of Anti-proliferative, Anti-oxidant and Anti-inflammatory Potential of the Antibacterial Peptide MFAP9

Raghavan, Rekha Mol Kollakalnaduvil; Pannippara, Manzur Ali; Kesav, Sapna; Mathew, A. G.; Bhat, Sarita G.; Rafeeq, C.M.; Elyas, K. K.

doi:10.1007/s10989-022-10442-w

Cited by 2 publications

(1 citation statement)

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“…Antimicrobial peptides are less likely to develop resistance than traditional antibiotics, and their antibacterial action is swifter [ 22 ]. They provide a safe and non-toxic effect, stability in highly acidic and alkaline environments, heat stability, broad-spectrum antibacterial properties, and antioxidant and free-radical-scavenging functions, which means that they can be widely used in medicine, food preservation, livestock breeding, and other industries [ 23 , 24 , 25 ].…”

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confidence: 99%

The Expression of Antibacterial Peptide Turgencin A in Pichia pastoris and an Analysis of Its Antibacterial Activity

Dong

Zhang

et al. 2023

Molecules

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Antibiotic resistance to pathogenic bacteria is becoming an increasing public health threat, and identifying alternatives to antibiotics would be an effective solution to the problem of drug resistance. Antimicrobial peptides are small peptides produced by various organisms; they are considered to be adequate antibiotic substitutes because they have intense, broad−spectrum antibacterial activity and stability, are widely available, and target strains do not quickly develop resistance. Recent research on antimicrobial peptides has shown that they have broad potential for applications in medicine, agriculture, food, and animal feed. Turgencin A is a potent antimicrobial peptide isolated from the Arctic sea squirt. We established a His-tagged expression system for Pichia pastoris and developed a rTurgencin A using the recombinant expression in Pichia pastoris with nickel column purification. This antimicrobial peptide showed intense antimicrobial activity against Gram-positive and Gram-negative bacteria and a good stability at most temperatures and pHs, as well as in various protease and salt ion concentrations, but underwent a significant decrease in stability in high-temperature and low-pH environments. Turgencin A induced bacterial membrane rupture, resulting in content leakage and subsequent cell death. It was also shown to have low hemolytic activity. This study provides primary data for the industrial production and application of the antimicrobial peptide Turgencin A.

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