• Corpus ID: 49361512

jmbReview Design and Engineering of Antimicrobial Peptides Based on LPcin-YK 3 , an Antimicrobial Peptide Derivative from Bovine Milk

@inproceedings{Kim2018jmbReviewDA,
  title={jmbReview Design and Engineering of Antimicrobial Peptides Based on LPcin-YK 3 , an Antimicrobial Peptide Derivative from Bovine Milk},
  author={Ji-sun Kim and Ji-ho Jeong and Yongae Kim},
  year={2018}
}

• Ji-sun Kim, Ji-ho Jeong, Yongae Kim
• Published 2018
• Biology

Since the discovery of penicillin by Alexander Fleming in 1929, antibiotics have been regarded as the most important discoveries in modern medicine, and in fact the development of antibiotics has exploded since the Second World War [1-3]. However, antibiotic resistance has been found in the early stages of development, and abuse of antibiotics in humans and livestock has led to the emergence of many multidrug-resistant bacteria or super bacteria [4]. As a result, the development of new antimicrobial agents to replace existing antibiotics that cause resistance problems is urgent, and antimicrobial peptides (AMPs) are emerging as new ones. Most AMPs are classified mainly on the basis of biochemical and structural characteristics, among which cationic AMPs have been found in animals, insects, and plants and have been known to play an important role in their innate host defense [5, 6]. Most cationic AMPs are composed of less than 50 amino acids and are positively charged with multiple lysine and arginine residues and have hydrophobic and amphipathic properties [7, 8]. The first reason for their attention as promising antimicrobial agents is their wide antimicrobial effect, including against gram-positive and gram-negative bacteria, fungi [9], protozoa [10], and enveloped viruses [11] and anticancer activity [12, 13]. The second is that they do not cause bacterial resistance problems because they exhibit antibiotic effects due to nonspecific electrostatic interactions with bacterial membrane lipid components [14, 15]. Although many native AMPs have been discovered and studied so far, they are rarely used as therapeutic agents despite the potential of such peptides. This is because of problems such as low antibiotic activity against fungi and bacteria, in vivo stability issues, or high production costs [16, 17]. Therefore, there is growing interest today in the design and development of new AMPs that have more antibiotic activity and are more secure to host cells, based on existing native AMPs. We have identified the relationship between the structure and activity of lactophoricin, a natural AMP found in bovine milk [18-20], and successfully designed, purified, Received: November 28, 2017 Revised: December 19, 2017 Accepted: December 20, 2017