Antimicrobial Activity of Snake β-Defensins and Derived Peptides
Abstract
:1. Introduction
2. Results
3. Discussion
4. Material and Methods
4.1. Molecular Modeling and Molecular Properties Calculation
4.2. Antibacterial Activity
4.3. Antifungal Activity
Author Contributions
Funding
Institutional Review Board Statement
Informed Consent Statement
Conflicts of Interest
References
- Mahlapuu, M.; Håkansson, J.; Ringstad, L.; Björn, C. Antimicrobial Peptides: An Emerging Category of Therapeutic Agents. Front. Cell. Infect. Microbiol. 2016, 6, 194. [Google Scholar] [CrossRef] [Green Version]
- Uhlig, T.; Kyprianou, T.; Martinelli, F.G.; Oppici, C.A.; Heiligers, D.; Hills, D.; Calvo, X.R.; Verhaert, P. The emergence of peptides in the pharmaceutical business: From exploration to exploitation. EuPA Open Proteom. 2014, 4, 58–69. [Google Scholar] [CrossRef] [Green Version]
- Gil-Gil, T.; Laborda, P.; Sanz-García, F.; Hernando-Amado, S.; Blanco, P.; Martínez, J.L. Antimicrobial resistance: A multifaceted problem with multipronged solutions. Microbiologyopen 2019, 8, e945. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Andrès, E. Cationic antimicrobial peptides in clinical development, with special focus on thanatin and heliomicin. Eur. J. Clin. Microbiol. Infect. Dis. 2012, 31, 881–888. [Google Scholar] [CrossRef]
- Wang, Y.; Hong, J.; Liu, X.; Yang, H.; Liu, R.; Wu, J.; Wang, A.; Lin, D.; Lai, R. Snake Cathelicidin from Bungarus fasciatus Is a Potent Peptide Antibiotics. PLoS ONE 2008, 3, e3217. [Google Scholar] [CrossRef] [Green Version]
- Blower, R.J.; Barksdale, S.M.; van Hoek, M.L. Snake Cathelicidin NA-CATH and Smaller Helical Antimicrobial Peptides Are Effective against Burkholderia thailandensis. PLoS Negl. Trop. Dis. 2015, 9, e0003862. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Zhao, F.; Lan, X.-Q.; Du, Y.; Chen, P.-Y.; Zhao, J.; Zhao, F.; Lee, W.-H.; Zhang, Y. King cobra peptide OH-CATH30 as a potential candidate drug through clinic drug-resistant isolates. Zool. Res. 2018, 39, 87–96. [Google Scholar] [PubMed] [Green Version]
- Barros, E.; Gonçalves, R.M.; Cardoso, M.H.; Santos, N.C.; Franco, O.L.; Cândido, E.S. Snake Venom Cathelicidins as Natural Antimicrobial Peptides. Front. Pharmacol. 2019, 10, 1415. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Carlile, S.R.; Shiels, J.; Kerrigan, L.; Delaney, R.; Megaw, J.; Gilmore, B.F.; Weldon, S.; Dalton, J.P.; Taggart, C.C. Sea snake cathelicidin (Hc-cath) exerts a protective effect in mouse models of lung inflammation and infection. Sci. Rep. 2019, 9, 6071. [Google Scholar] [CrossRef]
- Pérez-Peinado, C.; Dias, A.S.; Mendonça, D.A.; Castanho, M.A.R.B.; Veiga, A.S.; Andreu, D. Structural determinants conferring unusual long life in human serum to rattlesnake-derived antimicrobial peptide Ctn [15–34]. J. Pep. Sci. 2019, 25, e3195. [Google Scholar] [CrossRef] [PubMed]
- Dean, S.N.; Bishop, B.M.; van Hoek, M.L. Natural and synthetic cathelicidin peptides with anti-microbial and anti-biofilm activity against Staphylococcus aureus. BMC Microbiol. 2011, 11, 114. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Tajbakhsh, M.; Akhavan, M.M.; Fallah, F.; Karimi, A. A Recombinant Snake Cathelicidin Derivative Peptide: Antibiofilm Properties and Expression in Escherichia coli. Biomolecules 2018, 8, 118. [Google Scholar] [CrossRef] [Green Version]
- Samy, R.P.; Gopalakrishnakone, P.; Stiles, B.G.; Girish, K.S.; Swamy, S.N.; Hemshekhar, M.; Tan, K.S.; Rowan, E.G.; Sethi, G.; Chow, V.T.K. Snake Venom Phospholipases A2: A Novel Tool against Bacterial Diseases. Curr. Med. Chem. 2012, 19, 6150–6162. [Google Scholar] [CrossRef]
- Izidoro, L.F.M.; Sobrinho, J.C.; Mendes, M.M.; Costa, T.R.; Grabner, A.N.; Rodrigues, V.M.; da Silva, S.L.; Zanchi, F.B.; Zuliani, J.P.; Fernandes, C.F.C.; et al. Snake Venom L-Amino Acid Oxidases: Trends in Pharmacology and Biochemistry. Biomed. Res. Int. 2014, 2014, 196754. [Google Scholar] [CrossRef] [Green Version]
- Samy, R.P.; Gopalakrishnakone, P.; Chow, V.T.K.; Ho, B. Viper Metalloproteinase (Agkistrodon halys Pallas) with Antimicrobial Activity against Multi-Drug Resistant Human Pathogens. J. Cell. Physiol. 2008, 216, 54–68. [Google Scholar] [CrossRef] [PubMed]
- Yount, N.Y.; Kupferwasser, D.; Spisni, A.; Dutz, S.M.; Ramjan, Z.H.; Sharma, S.; Waring, A.J.; Yeaman, M.R. Selective reciprocity in antimicrobial activity versus cytotoxicity of hBD-2 and crotamine. Proc. Natl. Acad. Sci. USA 2009, 106, 14972–14977. [Google Scholar] [CrossRef] [Green Version]
- Oguiura, N.; Boni-Mitake, M.; Affonso, R.; Zhang, G. In vitro antibacterial and hemolytic activities of crotamine, a small basic myotoxin from rattlesnake Crotalus durissus. J. Antibiot. 2011, 64, 327–331. [Google Scholar] [CrossRef] [PubMed]
- Yamane, E.S.; Bizerra, F.C.; Oliveira, E.B.; Moreira, J.T.; Rajabi, M.; Nunes, G.L.C.; de Souza, A.O.; da Silva, I.D.C.G.; Yamane, T.; Karpel, R.L.; et al. Unraveling the antifungal activity of a South American rattlesnake toxin Crotamine. Biochimie 2013, 95, 231–240. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Lomonte, B.; Ângulo, Y.; Moreno, E. Synthetic Peptides Derived from the C-Terminal Region of Lys49 Phospholipase A2 Homologues from Viperidae Snake Venoms: Biomimetic Activities and Potential Applications. Curr. Pharm. Des. 2010, 16, 3224–3230. [Google Scholar] [CrossRef]
- Chen, W.; Yang, B.; Zhou, H.; Sun, L.; Dou, J.; Qian, H.; Huang, W.; Mei, Y.; Han, J. Structure–activity relationships of a snake cathelicidin-related peptide, BF-15. Peptides 2011, 32, 2497–2503. [Google Scholar] [CrossRef] [PubMed]
- Almeida, J.R.; Mendes, B.; Lancellotti, M.; Marangoni, S.; Vale, N.; Passos, O.; Ramos, M.J.; Fernandes, P.A.; Gomes, P.; Da Silva, S.L. A novel synthetic peptide inspired on Lys49 phospholipase A2 from Crotalus oreganus abyssus snake venom active against multidrug resistant clinical isolates. Eur. J. Med. Chem. 2018, 149, 248–256. [Google Scholar] [CrossRef] [PubMed]
- Falcao, C.B.; Radis-Baptista, G. Crotamine and crotalicidin, membrane active peptides from Crotalus durissus terrificus rattlesnake venom, and their structurally-minimized fragments for applications in medicine and biotechnology. Peptides 2020, 126, 170234. [Google Scholar] [CrossRef] [PubMed]
- Oguiura, N.; Boni-Mitake, M.; Rádis-Baptista, G. New view on crotamine, a small basic polypeptide myotoxin from South American rattlesnake venom. Toxicon 2005, 46, 363–370. [Google Scholar] [CrossRef] [PubMed]
- Coronado, M.A.; Gabdulkhakov, A.; Georgieva, D.; Sankaran, B.; Murakami, M.T.; Arni, R.K.; Betzel, C. Structure of the polypeptide crotamine from the Brazilian rattlesnake Crotalus durissus terrificus. Acta Cryst. 2013, D69, 1958–1964. [Google Scholar] [CrossRef] [Green Version]
- Rádis-Baptista, G.; Kubo, T.; Oguiura, N.; Silva, A.R.B.P.; Hayashi, M.A.F.; Oliveira, E.B.; Yamane, T. Identification of crotasin, a crotamine-related gene of Crotalus durissus terrificus. Toxicon 2004, 43, 751–759. [Google Scholar] [CrossRef]
- Corrêa, P.G.; Oguiura, N. Phylogenetic analysis of β-defensin-like genes of Bothrops, Crotalus and Lachesis snakes. Toxicon 2013, 69, 65–74. [Google Scholar] [CrossRef] [PubMed]
- Oliveira, Y.S.; Corrêa, P.G.; Oguiura, N. Beta-defensin genes of the Colubridae snakes Phalotris mertensi, Thamnodynastes hypoconia, and T. strigatus. Toxicon 2018, 146, 124–128. [Google Scholar] [CrossRef]
- Xiao, Y.; Cai, Y.; Bommineni, Y.R.; Fernando, S.C.; Prakash, O.; Gilliland, S.E.; Zhang, G. Identification and functional characterization of three chicken cathelicidins with potent antimicrobial activity. J. Biol. Chem. 2006, 281, 2858–2867. [Google Scholar] [CrossRef] [Green Version]
- Patani, G.A.; LaVoie, E.J. Bioisosterism: A Rational Approach in Drug Design. Chem. Rev. 1996, 96, 3147–3176. [Google Scholar] [CrossRef]
- Berman, H.M.; Westbrook, J.; Feng, Z.; Gilliland, G.; Bhat, T.N.; Weissig, H.; Shindyalov, I.N.; Bourne, P.E. The Protein Data Bank. Nucl. Acids Res. 2000, 28, 235–242. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Palomino, J.C.; Martin, A.; Camacho, M.; Guerra, H.; Swings, J.; Portaels, F. Resazurin microtiter assay plate: Simple and inexpensive method for detection of drug resistance in Mycobacterium tuberculosis. Antimicrob. Agents Chemother. 2002, 46, 2720–2722. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Dehghani, R.; Sharif, M.R.; Moniri, R.; Sharif, A.; Kashani, H.H. The identification of bacterial flora in oral cavity of snakes. Comp. Clin. Pathol. 2016, 25, 279–283. [Google Scholar] [CrossRef]
- Dehghani1, R.; Sharif, A.; Assadi, M.A.; Kashani, H.H.; Sharif, M.R. Fungal flora in the mouth of venomous and non-venomous snakes. Comp. Clin. Pathol. 2016, 25, 1207–1211. [Google Scholar] [CrossRef]
- Jorge, M.T.; Ribeiro, L.A. Infections in the bite site after envenoming by snakes of the Bothrops genus. J. Venom. Anim. Toxins 1997, 3, 264–272. [Google Scholar] [CrossRef]
- Garcia-Lima, E.; Laure, C.J. A study of bacterial contamination of rattlesnake venom. Rev. Soc. Bras. Med. Trop. 1987, 20, 19–21. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Bercovici, D.; Chudzinski, A.M.; Dias, W.O.; Esteves, M.I.; Hiraichi, E.; Oishi, N.Y.; Picarelli, Z.P.; Rocha, M.C.; Ueda, C.M.P.M.; Yamanouye, N.; et al. A systematic fraction of Crotalus durissus terrificus venom. Mem. Inst. Butantan 1987, 49, 69–78. [Google Scholar]
- Sharma, H.; Nagaraj, R. Human β-Defensin 4 with Non-Native Disulfide Bridges Exhibit Antimicrobial Activity. PLoS ONE 2015, 10, e0119525. [Google Scholar] [CrossRef] [Green Version]
- Liu, S.; Zhou, L.; Li, J.; Suresh, A.; Verma, C.; Foo, Y.H.; Yap, E.P.H.; Tan, D.T.H.; Beuerman, R.W. Linear Analogues of Human b-Defensin 3: Concepts for Design of Antimicrobial Peptides with Reduced Cytotoxicity to Mammalian Cells. ChemBioChem 2008, 9, 964–973. [Google Scholar] [CrossRef]
- Huang, X.-X.; Gao, C.-Y.; Zhao, Q.-J.; Li, C.-L. Antimicrobial Characterization of Site-Directed Mutagenesis of Porcine Beta Defensin 2. PLoS ONE 2015, 10, e0118170. [Google Scholar] [CrossRef]
- Samy, R.P.; Kandasamy, M.; Gopalakrishnakone, P.; Stiles, B.G.; Rowan, E.G.; Becker, D.; Shanmugam, M.K.; Sethi, G.; Chow, V.T.K. Wound Healing Activity and Mechanisms of Action of an Antibacterial Protein from the Venom of the Eastern Diamondback Rattlesnake (Crotalus adamanteus). PLoS ONE 2014, 9, e80199. [Google Scholar] [CrossRef] [Green Version]
- Samy, R.P.; Stiles, B.G.; Chinnathambi, A.; Zayed, M.E.; Alharbi, S.A.; Franco, O.L.; Rowan, E.G.; Kumar, A.P.; Lim, L.H.K.; Sethi, G. Viperatoxin-II: A novel viper venom protein as an effective bactericidal Agent. FEBS Open Bio. 2015, 5, 928–941. [Google Scholar] [CrossRef] [Green Version]
- Sudarshan, S.; Dhananjaya, B.L. Antibacterial Potential of a Basic Phospholipase A2 (VRV_PL_V) of Daboia russellii pulchella (Russell’s Viper) Venom. Biochemistry 2014, 79, 1237–1244. [Google Scholar] [CrossRef]
- Sudarshan, S.; Dhananjaya, B.L. Antibacterial Potential of a Basic Phospholipase A2 (VRV_PL_VIIIa) of Daboia russellii pulchella (Russell’s Viper) Venom. J. Venom. Anim. Toxins Incl. Trop. Dis. 2015, 21, 17. [Google Scholar] [CrossRef] [Green Version]
- Sudarshan, S.; Dhananjaya, B.L. The Antimicrobial Activity of an Acidic Phospholipase A2 (NN-XIa-PLA2) from the Venom of Naja naja naja (Indian Cobra). Appl. Biochem. Biotechnol. 2015, 176, 2027–2038. [Google Scholar] [CrossRef]
- Corrêa, E.A.; Kayano, A.M.; Diniz-Sousa, R.; Setúbal, S.S.; Zanchi, F.B.; Zuliani, J.P.; Matos, N.B.; Almeida, J.R.; Resende, L.M.; Marangoni, S.; et al. Isolation, structural and functional characterization of a new Lys49 phospholipase A2 homologue from Bothrops neuwiedi urutu with bactericidal potential. Toxicon 2016, 115, 13–21. [Google Scholar] [CrossRef] [PubMed]
- Guo, C.; Liu, S.; Yao, Y.; Zhang, Q.; Sun, M.-Z. Past decade study of snake venom L-amino acid oxidase. Toxicon 2012, 60, 302–311. [Google Scholar] [CrossRef] [PubMed]
- Muñoz, L.J.V.; Estrada-Gomez, S.; Núñez, V.; Sanz, L.; Calvete, J.J. Characterization and cDNA sequence of Bothriechis schlegelii l-aminoacid oxidase with antibacterial activity. Int. J. Biol. Macromol. 2014, 69, 200–207. [Google Scholar] [CrossRef]
- Costa, T.R.; Menaldo, D.L.; da Silva, C.P.; Sorrechia, R.; de Albuquerque, S.; Pietro, R.C.L.R.; Ghisla, S.; Antunes, L.M.G.; Sampaio, S.V. Evaluating the microbicidal, antiparasitic and antitumor effects of CR-LAAO from Calloselasma rhodostoma venom. Int. J. Biol. Macromol. 2015, 80, 489–497. [Google Scholar] [CrossRef] [PubMed]
- Falcao, C.B.; de La Torre, B.G.; Perez-Peinado, C.; Barron, A.E.; Andreu, D.; Radis-Baptista, G. Vipericidins: A novel family of cathelicidin-related peptides from the venom gland of South American pit vipers. Amino Acids 2014, 46, 2561–2571. [Google Scholar] [CrossRef]
- Wei, L.; Gao, J.; Zhang, S.; Wu, S.; Xie, Z.; Ling, G.; Kuang, Y.-Q.; Yang, Y.; Yu, H.; Wang, Y. Identification and Characterization of the First Cathelicidin from Sea Snakes with Potent Antimicrobial and Antiinflammatory Activity and Special Mechanism. J. Biol. Chem. 2015, 290, 16633–16652. [Google Scholar] [CrossRef] [Green Version]
- Lee, M.L.; Tan, N.H.; Fung, S.Y.; Sekaran, S.D. Antibacterial action of a heat-stable form of L-amino acid oxidase isolated from king cobra (Ophiophagus hannah) venom. Comp. Biochem. Physiol. C 2011, 153, 237–242. [Google Scholar] [CrossRef] [PubMed]
- Okubo, B.M.; Silva, O.N.; Migliolo, L.; Gomes, D.G.; Porto, W.F.; Batista, C.L.; Ramos, C.S.; Holanda, H.H.S.; Dias, S.C.; Franco, O.L.; et al. Evaluation of an Antimicrobial L-Amino Acid Oxidase and Peptide Derivatives from Bothropoides mattogrosensis Pitviper Venom. PLoS ONE 2012, 7, e33639. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Phua, C.S.; Vejayan, J.; Ambu, S.; Ponnudurai, G.; Gorajana, A. Purification and antibacterial activities of an L-amino acid oxidase from king cobra (Ophiophagus hannah) venom. J. Venom. Anim. Toxins Incl. Trop. Dis. 2012, 18, 198–207. [Google Scholar] [CrossRef] [Green Version]
- Skarnes, R.C. L-amino acid oxidase, a bacterial system. Nature 1970, 225, 1072. [Google Scholar] [CrossRef]
- Accary, C.; Hraoui-Bloquet, S.; Hamze, M.; Mallem, Y.; El Omar, F.; Sabatier, J.-M.; Desfontis, J.-C.; Fajloun, Z. Protein Content Analysis and Antimicrobial Activity of the Crude Venom of Montivipera bornmuelleri; a Viper from Lebanon. Infect. Disord. Drug Targets 2014, 14, 49–55. [Google Scholar] [CrossRef]
- Lai, Y.; Gallo, R.L. AMPed up immunity: How antimicrobial peptides have multiple roles in immune defense. Trends Immunol. 2009, 30, 131–141. [Google Scholar] [CrossRef] [Green Version]
- Alibardi, L. Granulocytes of Reptilian Sauropsids Contain Beta-Defensin-like Peptides: A Comparative Ultrastructural Survey. J. Morphol. 2013, 274, 877–886. [Google Scholar] [CrossRef]
- Alibardi, L.; Celeghin, A.; Dalla Valle, L. Wounding in lizards results in the release of beta-defensins at the wound site and formation of an antimicrobial barrier. Dev. Comp. Immunol. 2012, 36, 557–565. [Google Scholar] [CrossRef] [PubMed]
- Dorin, J.R.; Barratt, C.L.R. Importance of β-defensins in sperm function. Mol. Hum. Reprod. 2014, 20, 821–826. [Google Scholar] [CrossRef] [Green Version]
- Craik, D.J.; Fairlie, D.P.; Liras, S.; Price, D. The Future of Peptide-based Drugs. Chem. Biol. Drug Des. 2013, 81, 136–147. [Google Scholar] [CrossRef] [PubMed]
- Hoover, D.M.; Wu, Z.; Tucker, K.; Lu, W.; Lubkowski, J. Antimicrobial Characterization of Human β-Defensin 3 Derivatives. Antimicrob. Agents Chemother. 2003, 47, 2804–2809. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Sudheendra, U.S.; Dhople, V.; Datta, A.; Kar, R.K.; Shelburne, C.E.; Bhunia, A.; Ramamoorthy, A. Membrane disruptive antimicrobial activities of human β-defensin-3 analogs. Eur. J. Med. Chem. 2015, 91, 91–99. [Google Scholar] [CrossRef] [Green Version]
- Scudiero, O.; Nigro, E.; Cantisani, M.; Colavita, I.; Leone, M.; Mercurio, F.A.; Galdiero, M.; Pessi, A.; Daniele, A.; Salvatore, F.; et al. Design and activity of a cyclic mini-β-defensin analog: A novel antimicrobial tool. Int. J. Nanomed. 2015, 10, 6523–6539. [Google Scholar]
- Saravanan, R.; Li, X.; Lim, K.; Mohanram, H.; Peng, L.; Mishra, B.; Basu, A.; Lee, J.-M.; Bhattacharjya, S.; Leong, S.S.J. Design of Short Membrane Selective Antimicrobial Peptides Containing Tryptophan and Arginine Residues for Improved Activity, Salt-Resistance, and Biocompatibility. Biotechnol. Bioeng. 2014, 111, 37–49. [Google Scholar] [CrossRef]
- Wessolowski, A.; Bienert, M.; Dathe, M. Antimicrobial activity of arginine- and tryptophan-rich hexapeptides: The effects of aromatic clusters, d-amino acid substitution and cyclization. J. Pept. Res. 2004, 64, 159–169. [Google Scholar] [CrossRef] [PubMed]
- Dal Mas, C.; Pinheiro, D.A.; Campeiro, J.D.; Mattei, B.; Oliveira, V.; Oliveira, E.B.; Miranda, A.; Perez, K.R.; Hayashi, M.A.F. Biophysical and biological properties of small linear peptides derived from crotamine, a cationic antimicrobial/antitumoral toxin with cell penetrating and cargo delivery abilities. Biochim. Biophys. Acta Biomembr. 2017, 1859, 2340–2349. [Google Scholar] [CrossRef]
- Ponnappan, N.; Budagavi, D.P.; Chugh, A. CyLoP-1: Membrane-active peptide with cell-penetrating and antimicrobial properties. Biochim. Biophys. Acta 2017, 1859, 167–176. [Google Scholar] [CrossRef] [PubMed]
- Mandal, M.; Jagannadham, M.V.; Nagaraj, R. Antibacterial activities and conformations of bovine β-defensin BNBD-12 and analogs:structural and disulfide bridge requirements for activity. Peptides 2002, 23, 413–418. [Google Scholar] [CrossRef]
- Hilpert, K.; Elliott, M.R.; Volkmer-Engert, R.; Henklein, P.; Donini, O.; Zhou, Q.; Winkler, D.F.H.; Hancock, R.E.W. Sequence requirements and an optimization strategy for short antimicrobial peptides. Chem. Biol. 2006, 13, 1101–1107. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Mookherjee, N.; Anderson, M.A.; Haagsman, H.P.; Davidson, D.J. Antimicrobial host defence peptides: Functions and clinical potential. Nat. Rev. Drug Discov. 2020, 19, 311–332. [Google Scholar] [CrossRef]
- Stone, K.L.; Williams, K.R. Enzymatic digestion of proteins in solutions and in SDS polyacrylamide gel. In The Protein Protocol Handbook; Walker, J.M., Ed.; Human Press Inc.: Totowa, NJ, USA, 1996; pp. 415–421. [Google Scholar]
- Boni-Mitake, M.; Costa, H.; Spencer, P.J.; Vassillieff, V.S.; Rogero, J.R. Effects of 60Co gamma radiation on crotamine. Braz. J. Med. Biol. Res. 2001, 34, 1531–1538. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Petersen, T.N.; Brunak, S.; von Heijne, G.; Nielsen, H. SignalP 4.0: Discriminating signal peptides from transmembrane regions. Nat. Methods 2011, 8, 785–786. [Google Scholar] [CrossRef] [PubMed]
- Breneman, C.M.; Wiberg, K.B. Determining atom-centered monopoles from molecular electrostatic potentials.The need for high sampling density in formamide conformational analysis. J. Comput. Chem. 1990, 11, 361–373. [Google Scholar] [CrossRef]
- Clinical and Laboratory standards Institute (CLSI). Reference Method for Broth Dilution Antifungal Susceptibility Testing of Yeasts, 4th ed.; CLSI Standard M27; Clinical and Laboratory standards Institute: Wayne, PA, USA, 2017. [Google Scholar]
MIC (µM) | ||||
---|---|---|---|---|
Samples | E. coli | M. luteus | C. freundii | S. aureus |
Crotamine (+7) | 13.3 | 1.7 | 6.7 | >105 |
Linear crotamine | 26.6 | 1.7 | 26.7 | >105 |
DefbBm02 (+11) | 3.2 | 0.8 | 1.6 | 12.8 |
DefbBm03 (+10) | 1.6 | 1.6 | 3.2 | >103 |
DefbBd03 (+6) | >115 | 0.9 | >115 | >115 |
DefbBj01 (+4) | >105 | 3.2 | >105 | >105 |
DefbBju01 (+7) | >111 | >111 | >111 | >111 |
DefbBn02 (+2) | >113 | >113 | >113 | >113 |
DefbLm01 (+2) | >113 | 28.4 | >113 | >113 |
DefbLm02 (+8) | 3.4 | 0.9 | 3.4 | 6.8 |
DefbPm (+6) | >109 | 6.8 | >109 | >109 |
DefbTs (+3) | >122 | 15.3 | >122 | >122 |
hBd02 (+6) | 15.6 | 2 | >124 | >124 |
Crotasin (−1) | >108 | >108 | >108 | >108 |
Peptide | Derived from | Sequence | Hidrofobicity (Kcal/mol) | Net Charge | MW (Da) |
---|---|---|---|---|---|
PS1 (13 aa) | Crotamine | SRWRWKSSKKGSG | +19.88 | +5 | 1549 |
PS2 (14 aa) | defbBm02 | SQMGRMSSRRRFGK | +19.34 | +5 | 1683 |
PS3 (12 aa) | defbLm02 | SGPGRRSSRRRK | +23.57 | +6 | 1399 |
PS4 (14 aa) | defbBm03 | SQMGQMSSRRRFGK | +18.30 | +4 | 1655 |
PS5 (13 aa) | PS3 | SGPGRRSSRRRWK | +21.48 | +6 | 1585 |
PS6 (7 aa) | PS1 | SRWRWKS | +11.06 | +3 | 1005 |
MIC (µM) | |||||
---|---|---|---|---|---|
Peptides | E. coli | S. aureus | M. luteus | K. pneumoniae | C. freundii |
PS1 | 56.5 | 56.5 | 28.4 | >452 | 113 |
PS2 | 415 | 415 | 26.1 | >415 | >415 |
PS3 | >500 | 125 | 31.5 | >500 | >500 |
PS4 | >423 | >423 | 26.6 | >423 | >423 |
PS5 | 55.2 | 27.7 | 13.9 | 27.7 | 110 |
PS6 | 697 | 349 | 43.8 | >697 | >697 |
MIC90 (µM) | ||||
---|---|---|---|---|
Peptides | Candida albicans | Cryptococcus neoformans | Trichophyton rubrum | Aspergillus fumigatus |
PS1 | >250 | >250 | >250 | >250 |
PS2 | >250 | >250 | >250 | >250 |
PS3 | >250 | >250 | >250 | >250 |
PS4 | >250 | >250 | >250 | >250 |
PS5 | >250 | >250 | >250 | >250 |
PS6 | >250 | >250 | >250 | >250 |
Peptide/ Snake | GenBank Accession Number | Amino Acid Sequence | Hidrofobicity Kcal/mol | Net Charge at pH 7 | MW Da |
---|---|---|---|---|---|
Crotamine/ C. durissus | YKQCHKKGGHCFPKEKICLPPSSDFGKMDCRWRWKCCKKGSG | +49.14 | +8 | 4886 | |
Crotasin/ C. durissus | AF250212 | QPQCRWLDGFCHSSPCPSGTTSIGQQDCLWYESCCIPRYEK | +28.91 | −1 | 4708 |
defbBd03/ B. diporus | KC117160 | QPECLRQGGMCRPRLCPYVSLGQLDCQNGHVCCRKKPRK | +37.08 | +5 | 4456 |
defbBj/ B. jararaca | KC117163 | QEECLQQGGFCRLIRCPFGYDSLEQQDCRKGQRCCIRKPRK | +45.05 | +4 | 4874 |
defbBju/ B. jararacussu | KC117165 | QRRCHQKGGMCLPGPCPPGYDSLGQQDCRRGQKCCIKRFGK | +43.85 | +7 | 4591 |
defbBm02/ B. mattogrossensis | KC117167 | QRRCRQRRGICRPRPCPPENFSLGRLDCQMGRMCCRRRFGK | +39.97 | +11 | 4978 |
defbBm03/ B. mattogrossensis | KC117168 | QRRCRQRRGICRPRPCPPENFSLGRLDCQMGQMCCRRRFGK | +38.93 | +10 | 4950 |
defbBn02/ B. neuwiedi | KC117169 | QPECCQEGGICHSKQCPLGYSSLGRLDCQLGQRCCIRIFGK | +33.65 | +2 | 4513 |
defbLm01/ L. muta | KC117171 | QEWCRGLGGFCSFYQCRPGHDLGPQDCWPERRCCRWGK | +33.69 | +2 | 4515 |
defbLm02/ L. muta | KC117172 | QGQCHQQRGRCFLHQCPLSHYFLGRLDCGPGRRCCRRRK | +36.90 | +8 | 4655 |
defbPm/ P. mertensis | KX664436 | QRICLGGRGFCHSTPCPRSTIDYGKKDCWGSLRCCEPKRPGK | +42.13 | +6 | 4695 |
defbTs/ T. strigatus | KX664429 | QDLCHNLGGRCFRNRCSWSLRNHGGQDCPWGSVCCKP | +31.16 | +3 | 4188 |
hBD02/ Human | AF071216 | DPVTCLKSGAICHPVFCPRRYKQIGTCGLPGTKCCKKP | +31.07 | +6 | 4104 |
Publisher’s Note: MDPI stays neutral with regard to jurisdictional claims in published maps and institutional affiliations. |
© 2021 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).
Share and Cite
Oguiura, N.; Corrêa, P.G.; Rosmino, I.L.; de Souza, A.O.; Pasqualoto, K.F.M. Antimicrobial Activity of Snake β-Defensins and Derived Peptides. Toxins 2022, 14, 1. https://0-doi-org.brum.beds.ac.uk/10.3390/toxins14010001
Oguiura N, Corrêa PG, Rosmino IL, de Souza AO, Pasqualoto KFM. Antimicrobial Activity of Snake β-Defensins and Derived Peptides. Toxins. 2022; 14(1):1. https://0-doi-org.brum.beds.ac.uk/10.3390/toxins14010001
Chicago/Turabian StyleOguiura, Nancy, Poliana Garcia Corrêa, Isabella Lemos Rosmino, Ana Olívia de Souza, and Kerly Fernanda Mesquita Pasqualoto. 2022. "Antimicrobial Activity of Snake β-Defensins and Derived Peptides" Toxins 14, no. 1: 1. https://0-doi-org.brum.beds.ac.uk/10.3390/toxins14010001