Design and Engineering of Antimicrobial Peptides Based on LPcin-YK3, an Antimicrobial Peptide Derivative from Bovine Milk
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We have previously derived a novel antimicrobial peptide, LPcin-YK3(YK3), based on lactophoricin and have successfully studied and reported on the relationship between its structure and function. In this study, antimicrobial peptides with improved antimicrobial activity, less cytotoxicity, and shorter length were devised and characterized on the basis of YK3, and named YK5, YK8, and YK11. The peptide design was based on a variety of knowledge, and a total of nine analog peptides consisted of one to three amino acid substitutions and C-terminal deletions. In detail, tryptophan substitution improved the membrane perturbation, lysine substitution increased the net charge, and excessive amphipathicity decreased. The analog peptides were examined for structural characteristics through spectroscopic analytical techniques, and antimicrobial susceptibility tests were used to confirm their activity and safety. We expect that these studies will provide a platform for systematic engineering of new antibiotic peptides and generate libraries of various antibiotic peptides.
Abstract
We have previously derived a novel antimicrobial peptide, LPcin-YK3(YK3), based on lactophoricin and have successfully studied and reported on the relationship between its structure and function. In this study, antimicrobial peptides with improved antimicrobial activity, less cytotoxicity, and shorter length were devised and characterized on the basis of YK3, and named YK5, YK8, and YK11. The peptide design was based on a variety of knowledge, and a total of nine analog peptides consisted of one to three amino acid substitutions and C-terminal deletions. In detail, tryptophan substitution improved the membrane perturbation, lysine substitution increased the net charge, and excessive amphipathicity decreased. The analog peptides were examined for structural characteristics through spectroscopic analytical techniques, and antimicrobial susceptibility tests were used to confirm their activity and safety. We expect that these studies will provide a platform for systematic engineering of new antibiotic peptides and generate libraries of various antibiotic peptides.
참고문헌 (39)
- Chicarelli-Robinson M, "Plants and microbes as complementary sources of chemical diversity for drug discovery;Phytochemical Diversity: A Source of New Industrial Products", pp.57~83 (1997)
- Georgopapadakou NH, "Antifungal agents: Chemotherapeutic targets and immunologic strategies", Antimicrob. Agents Chemother., 40, pp.279~291 (1996)
- Govender T, "Antimicrobial properties of the skin secretions of frogs", S. Afr. J. Sci., 108, pp.1~6 (2012)
- Walsh C, "Introduction: antibiotic resistance", Chem. Rev., 105, pp.391~394 (2015)
- Marshall SH, "Antimicrobial peptides: a natural alternative to chemical antibiotics and a potential for applied biotechnology", Electron J. Biotechnol., 6, pp.271~284 (2003)
- Hancock REW, "Cationic peptides: effectors in innate immunity and novel antimicrobials", Lancet Infect. Dis., 1, pp.156~164 (2001)[DOI]
- Jenssen H, "Peptide antimicrobial agents", Clin. Microbiol. Rev., 19, pp.491~511 (2006)
- Pistolesi S, "Membrane insertion and bilayer perturbation by antimicrobial peptide CM15", Biophys. J., 93, pp.1651~1660 (2007)
- Mohammad FV, "Bidesmosidic triterpenoidal saponins from the roots of Symphytum officinale", Planta Med., 61, pp.94~ (1995)
- Aley SB, "Killing of Giardia lamblia by cryptdins and cationic neutrophil peptides", Infect. Immun., 62, pp.5397~5403 (1994)
- Murakami T, "Direct virus inactivation of tachyplesin I and its isopeptides from horseshoe crab hemocytes", Chemotherapy, 37, pp.327~334 (1991)[DOI]
- Baker MA, "Anticancer efficacy of magainin 2 and analogue peptides", Cancer Res., 53, pp.3052~3057 (1993)
- Johnstone SA, "In vitro characterization of the anticancer activity of membrane-active cationic peptides. I. Peptide-mediated cytotoxicity and peptide-enhanced cytotoxic activity of doxorubicin against wild-type and P-glycoprotein over-expressing tumor cell lines", Anticancer Drug Des., 15, pp.151~160 (2000)
- Auvynet C, "Multifunctional host defense peptides: antimicrobial peptides, the small yet big players in innate and adaptive immunity", FEBS J., 276, pp.6497~6508 (2009)[DOI]
- Takahashi D, "Structural determinants of host defense peptides for antimicrobial activity and target cell selectivity", Biochimie, 92, pp.1236~1241 (2010)[DOI]
- Hancock REW, "Peptide antibiotics", Antimicrob. Agents Chemother., 43, pp.1317~1323 (1999)
- Brogden NK, "Will new generations of modified antimicrobial peptides improve their potential as pharmaceuticals?", Int. J. Antimicrob. Agents, 38, pp.217~225 (2011)
- Park TJ, "Cloning expression, isotope labeling, purification and characterization of bovine antimicrobial peptide, lactophoricin in Escherichia coli", Protein Expr. Purif., 65, pp.23~29 (2009)
- 김용애, "Optimized Methods for purification and NMR measurement of antibacterial peptide, bovine lactophoricin", Journal of the Korean Magnetic Resonance Society, 13(2), pp.96~107 (2009), 한국자기공명학회
- Park TJ, "Solution and solid-state NMR structural studies of antimicrobial peptides LPcin-I and LPcin-II", Biophys. J., 101, pp.1193~1201 (2011)[DOI]
- 김지선, "Optimized Expression and Characterization of Antimicrobial Peptides, LPcin Analogs", Bulletin of the Korean Chemical Society, 36(4), pp.1148~1154 (2015), 대한화학회[DOI]
- Jeong JH, "NMR structural studies of antimicrobial peptides: LPcin analogs", Biophys. J., 110, pp.423~430 (2016)[DOI]
- 김지선, "Design, Characterization, and Antimicrobial Activity of a Novel Antimicrobial Peptide Derived from Bovine Lactophoricin", Journal of Microbiology and Biotechnology, 27(4), pp.759~767 (2017), 한국미생물·생명공학회[DOI]
- Zhang SK, "Design of an <TEX>$\alpha$<", TEX>-helical antimicrobial peptide with improved cell-selective and potent anti-biofilm activity, 2016, pp.8, 27394~
- Matsuzaki K, "Why and how are peptide-lipid interactions utilized for self-defence? Magainins and tachyplesins as archetypes", Biochim. Biophys. Acta, 1462, pp.1~10 (1999)[DOI]
- Chan DI, "Tryptophan- and arginine-rich antimicrobial peptides: structures and mechanisms of action", Biochim. Biophys. Acta, 1758, pp.1184~1202 (2006)[DOI]
- Schibli DJ, "Tryptophan-rich antimicrobial peptides: comparative properties and membrane interactions", Biochem. Cell Biol., 80, pp.667~677 (2002)
- Bi X, "Investigation of the role of tryptophan residues in cationic antimicrobial peptides to determine the mechanism of antimicrobial action", J. Appl. Microbiol., 115, pp.663~672 (2013)[DOI]
- Zhu X, "Design of imperfectly amphipathic <TEX>$\alpha$<", TEX>-helical antimicrobial peptides with enhanced cell selectivity, 2014, pp.10, 244~257
- Chen Y, "Role of peptide hydrophobicity in the mechanism of action of <TEX>$\alpha$<", TEX>-helical antimicrobial peptides, 2007, pp.51, 1398~1406
- Tossi A, "Amphipathic, alpha-helical antimicrobial peptides", Biopolymers, 55, pp.4~30 (2000)[DOI]
- Giangaspero A, "Amphipathic alpha helical antimicrobial peptides", Eur. J. Biochem., 268, pp.5589~5600 (2001)[DOI]
- Won HS, "Systematic peptide engineering and structural characterization to search for the shortest antimicrobial peptide analogue of gaegurin 5", J. Biol. Chem., 279, pp.14784~14791 (2004)[DOI]
- Wieprecht T, "Modulation of membrane activity of amphipathic, antibacterial peptides by slight modifications of the hydrophobic moment", FEBS Lett., 417, pp.135~140 (1997)[DOI]
- Kondejewski LH, "Dissociation of antimicrobial and hemolytic activities in cyclic peptide diastereomers by systematic alterations in amphipathicity", J. Biol. Chem., 274, pp.13181~13192 (1999)[DOI]
- Nichols M, "Dynamic turn conformation of a short tryptophan-rich cationic antimicrobial peptide and its interaction with phospholipid membranes", J. Phys. Chem. B, 117, pp.14697~14708 (2013)[DOI]
- Joshi S, "N-terminal aromatic tag induced self assembly of tryptophan-arginine rich ultra short sequences and their potent antibacterial activity", RSC Adv., 5, pp.68610~68620 (2015)[DOI]
- Stromstedt AA, "Evaluation of strategies for improving proteolytic resistance of antimicrobial peptides by using variants of EFK17, an internal segment of LL-37", Antimicrob. Agents Chemother., 53, pp.593~602 (2009)
- Nguyen LT, "Serum stabilities of short tryptophan- and arginine-rich antimicrobial peptide analogs", PLoS One, 5, pp.e12684~ (2010)[DOI]