References
- Hancock REW, Nijnik A, Philpott DJ. 2012. Modulating immunity as a therapy for bacterial infections. Nat. Rev. Microbiol. 10: 243-254. https://doi.org/10.1038/nrmicro2745
- Haney EF, Mansour SC, Hancock REW. 2017. Antimicrobial peptides: an introduction, pp. 3-22. In Hansen P (ed.). Antimicrobial Peptides. Methods in Molecular Biology, Vol. 1548. Humana Press, New York.
- Koehbach J. 2017. Structure-activity relationships of insect defensins. Front. Chem. 5: 45. https://doi.org/10.3389/fchem.2017.00045
- Yi HY, Chowdhury M, Huang YD, Yu XQ. 2014. Insect antimicrobial peptides and their applications. Appl. Microbiol. Biotechnol. 98: 5807-5822. https://doi.org/10.1007/s00253-014-5792-6
- Kim SR, Hong MY, Park SW, Choi KH, Yun EY, Goo TW, et al. 2010. Characterization and cDNA cloning of a cecropin- like antimicrobial peptide, papiliocin, from the swallowtail butterfly, Papilio xuthus. Mol. Cells 29: 419-423. https://doi.org/10.1007/s10059-010-0050-y
- Kim JK, Lee E, Shin S, Jeong KW, Lee JY, Bae SY, et al. 2011. Structure and function of papiliocin with antimicrobial and anti-inflammatory activities isolated from the swallowtail butterfly, Papilio xuthus. J. Biol. Chem. 286: 41296-41311. https://doi.org/10.1074/jbc.M111.269225
- Lee J, Hwang JS, Hwang B, Kim JK, Kim SR, Kim Y, et al. 2010. Influence of the papiliocin peptide derived from Papilio xuthus on the perturbation of fungal cell membranes. FEMS Microbiol Lett. 311: 70-75. https://doi.org/10.1111/j.1574-6968.2010.02073.x
- Lee E, Kim JK, Jeon D, Jeong KW, Shin A, Kim Y. 2015. Functional roles of aromatic residues and helices of papiliocin in its antimicrobial and anti-inflammatory activities. Sci. Rep. 5: 12048. https://doi.org/10.1038/srep12048
- Jeon D, Jacob D, Kwak C, Kim Y. 2017. Short antimicrobial peptides exhibiting antibacterial and anti-inflammatory activities derived from the N-terminal helix of papiliocin. Bull. Korean Chem. Soc. 38: 1260-1268. https://doi.org/10.1002/bkcs.11277
- Bowdish DM, Davidson DJ, Scott MG, Hancock RE. 2005. Immunomodulatory activities of small host defense peptides. Antimicrob. Agents Chemother. 49: 1727-1732. https://doi.org/10.1128/AAC.49.5.1727-1732.2005
- Rosenfeld Y, Papo N, Shai Y. 2006. Endotoxin (lipopoly- saccharide) neutralization by innate immunity host-defense peptides. Peptide properties and plausible modes of action. J. Biol. Chem. 281: 1636-1643. https://doi.org/10.1074/jbc.M504327200
- Nell MJ, Tjabringa GS, Wafelman AR, Verrijk R, Hiemstra PS, Drijfhout JW, et al. 2006. Development of novel LL-37 derived antimicrobial peptides with LPS and LTA neutralizing and antimicrobial activities for therapeutic application. Peptides 27: 649-660. https://doi.org/10.1016/j.peptides.2005.09.016
- Frohm M, Agerberth B, Ahangari G, Stâhle-Bäckdahl M, Lidén S, Wigzell H, et al. 1997. The expression of the gene coding for the antibacterial peptide LL-37 is induced in human keratinocytes during inflammatory disorders. J. Biol. Chem. 272: 15258-15263. https://doi.org/10.1074/jbc.272.24.15258
- Lee PH, Ohtake T, Zaiou M, Murakami M, Rudisill JA, Lin KH, et al. 2005. Expression of an additional cathelicidin antimicrobial peptide protects against bacterial skin infection. Proc. Natl. Acad. Sci. USA 102: 3750-3755. https://doi.org/10.1073/pnas.0500268102
- Brandenburg K, Heinbockel L, Correa W, Lohner K. 2016. Peptides with dual mode of action: killing bacteria and preventing endotoxin-induced sepsis. Biochim. Biophys. Acta 1858: 971-979. https://doi.org/10.1016/j.bbamem.2016.01.011
- Terayama T, Yamakawa K, Umemura Y, Aihara M, Fujimi S. 2017. Polymyxin B hemoperfusion for sepsis and septic shock: a systematic review and meta-analysis. Surg. Infect. 18: 225-233. https://doi.org/10.1089/sur.2016.168
- Lee E, Kim JK, Shin S, Jeong KW, Shin A, Lee J, et al. 2013. Insight into the antimicrobial activities of coprisin isolated from the dung beetle, Copris tripartitus, revealed by structure-activity relationships. Biochim. Biophys. Acta 1828: 271-283. https://doi.org/10.1016/j.bbamem.2012.10.028
- Jeon D, Jeong MC, Jacob B, Bang JK, Kim EH, Cheong C, et al. 2017. Investigation of cationicity and structure of pseudin-2 analogues for enhanced bacterial selectivity and anti-inflammatory activity. Sci. Rep. 7: 1455. https://doi.org/10.1038/s41598-017-01474-0
- Green LC, Wagner DA, Glogowski J, Skipper PL, Wishnok JS, Tannenbaum SR. 1982. Analysis of nitrate, nitrite, and [15N]nitrate in biological fluids. Anal. Biochem. 126: 131-138. https://doi.org/10.1016/0003-2697(82)90118-X
- Jnawali HN, Lee E, Jeong KW, Shin A, Heo YS, Kim Y. 2014. Anti-inflammatory activity of rhamnetin and a model of its binding to c-Jun NH2-terminal kinase 1 and p38 MAPK. J. Nat. Prod. 77: 258-263. https://doi.org/10.1021/np400803n
- Trott O, Olson AJ. 2010. AutoDock Vina: improving the speed and accuracy of docking with a new scoring function, efficient optimization, and multithreading. J. Comput. Chem. 31: 455-461.
- Dassault Systemes BIOVIA. 2015. Discovery Studio, 4.1. Dassault Systemes, San Diego.
- Lee CC, Avalos AM, Ploegh HL. 2012. Accessory molecules for Toll-like receptors and their function. Nat. Rev. Immunol. 12: 168-179. https://doi.org/10.1038/nri3151
- Kondo T, Kawai T, Akira S. 2012. Dissecting negative regulation of Toll-like receptor signaling. Trends Immunol. 33.9: 449-458. https://doi.org/10.1016/j.it.2012.05.002
- O'Neill LA, Bryant CE, Doyle SL. 2009. Therapeutic targeting of Toll-like receptors for infectious and inflammatory diseases and cancer. Pharmacol. Rev. 61: 177-197. https://doi.org/10.1124/pr.109.001073
- Bhunia A, Domadia PN, Torres J, Hallock KJ, Ramamoorthy A, Bhattacharjya S. 2010. NMR structure of pardaxin, a pore- forming antimicrobial peptide, in lipopolysaccharide micelles: mechanism of outer membrane permeabilization. J. Biol. Chem. 285: 3883-3895. https://doi.org/10.1074/jbc.M109.065672
-
Sudheendra US, Dhople V, Datta A, Kar RK, Shelburne CE, Bhunia A, et al. 2014. Membrane disruptive antimicrobial activities of human
${\beta}$ -defensin-3 analogs. Eur. J. Med. Chem. 91: 91-99. - Baek MH, Kamiya M, Kushibiki T, Nakazumi T, Tomisawa S, Abe C, et al. 2016. Lipopolysaccharide-bound structure of the antimicrobial peptide cecropin P1 determined by nuclear magnetic resonance spectroscopy. J. Pept. Sci. 22: 214-221. https://doi.org/10.1002/psc.2865
-
Ghosh A, Bera S, Shai Y, Mangoni ML, Bhunia A. 2016. NMR structure and binding of esculentin-1a(1-21)
$NH_2$ and its diastereomer to lipopolysaccharide: correlation with biological functions. Biochim. Biophys. Acta 1858: 800-812. https://doi.org/10.1016/j.bbamem.2015.12.027 - Kushibiki T, Kamiya M, Aizawa T, Kumaki Y, Kikukawa T, Mizuguchi M, et al. 2014. Interaction between tachyplesin I, an antimicrobial peptide derived from horseshoe crab, and lipopolysaccharide. Biochim. Biophys. Acta 1844: 527-534. https://doi.org/10.1016/j.bbapap.2013.12.017