An overview of brevinin superfamily: Structure, function and clinical perspectives

Advances in Experimental Medicine and Biology

Volumn 818, Issue , 2014, Pages 197-212

  Savelyeva, Anna ^a,b   Ghavami, Saeid ^c   Davoodpour, Padideh ^d   Asoodeh, Ahmad ^e   Łos, Marek J ^d,f,g  

^a INSTITUTE OF CHEMICAL BIOLOGY AND FUNDAMENTAL MEDICINE   (Russian Federation)

^b NOVOSIBIRSK STATE UNIVERSITY   (Russian Federation)

^c UNIVERSITY OF MANITOBA   (Canada)

^d UPPSALA UNIVERSITY   (Sweden)

^e FERDOWSI UNIVERSITY OF MASHHAD   (Iran)

^f LINKÖPING UNIVERSITY   (Sweden)

^g POMERANIAN MEDICAL UNIVERSITY   (Poland)

Author keywords

Amidophosphoribosyltransferase; Bionanomaterials; Brevinin; Bufodienolides; Bufogenines; Cathepsin; Esculentin; Hypoglycemia; Japonicin; Magainins; Nanocarrier; Nigrocin; Palustrin; Peptidomimetica; Phosphatidylserines; Rana box; Ranacyclin; Ranalexin; Ranateurin; Ranid frogs; Temporin

Indexed keywords

AMIDOPHOSPHORIBOSYLTRANSFERASE; BREVININ; BREVININ 1CBB; BREVININ 2R; CISPLATIN; DOXORUBICIN; GAMMA INTERFERON; GASTRIC INHIBITORY POLYPEPTIDE; GLUCAGON LIKE PEPTIDE 1; GLUTATHIONE TRANSFERASE; INTEIN; INTERLEUKIN 8; NANOMATERIAL; POLYPEPTIDE ANTIBIOTIC AGENT; THIOREDOXIN; TUMOR NECROSIS FACTOR ALPHA; UNCLASSIFIED DRUG; AMPHIBIAN PROTEIN; ANTIMICROBIAL CATIONIC PEPTIDE; ANTINEOPLASTIC AGENT; ANTIVIRUS AGENT;

AMINO ACID SUBSTITUTION; ANTIBACTERIAL ACTIVITY; ANTINEOPLASTIC ACTIVITY; ANTIVIRAL ACTIVITY; APOPTOSIS; CANDIDA ALBICANS; CYTOKINE RELEASE; DRUG CYTOTOXICITY; ESCHERICHIA COLI; GENETIC ORGANIZATION; INSULIN RELEASE; MINIMUM INHIBITORY CONCENTRATION; MOLECULAR CLONING; NONHUMAN; PHYLOGENY; PRIORITY JOURNAL; REVIEW; STAPHYLOCOCCUS AUREUS; ANIMAL; CHEMISTRY; GENETICS; HUMAN; METABOLISM; PHYSIOLOGY; PROTEIN PROCESSING; STRUCTURE ACTIVITY RELATION;

AMPHIBIAN PROTEINS; ANIMALS; ANTIMICROBIAL CATIONIC PEPTIDES; ANTINEOPLASTIC AGENTS; ANTIVIRAL AGENTS; HUMANS; PHYLOGENY; PROTEIN PROCESSING, POST-TRANSLATIONAL; STRUCTURE-ACTIVITY RELATIONSHIP;

EID: 84921630327     PISSN: 00652598     EISSN: 22148019     Source Type: Book Series    
DOI: 10.1007/978-1-4471-6458-6_10     Document Type: Review

References (61)

1. Clarke BT (1997) The natural history of amphibian skin secretions, their normal functioning and potential medical applications. Biol Rev Camb Philos Soc 72(3):365-379
2. Duellman WE, Trueb L (1994) Biology of amphibians. Johns Hopkins University Press, Baltimore
3. Preusser HJ, Habermehl G, Sablofski M, Schmall-Haury D (1975) Antimicrobial activity of alkaloids from amphibian venoms and effects on the ultrastructure of yeast cells. Toxicon: Off J Int Soc Toxinol 13(4):285-289
4. Daly JW, Myers CW, Whittaker N (1987) Further classification of skin alkaloids from neotropical poison frogs (Dendrobatidae), with a general survey of toxic/noxious substances in the amphibia. Toxicon: Off J Int Soc Toxinol 25(10):1023-1095
5. Habermehl GG (1981) Venomous animals and their toxins. Springer, Berlin
6. Zasloff M (1987) Magainins, a class of antimicrobial peptides from xenopus skin: isolation, characterization of two active forms, and partial cDNA sequence of a precursor. Proc Natl Acad Sci U S A 84(15):5449-5453
7. Bevins CL, ZasloffM(1990) Peptides from frog skin. Annu Rev Biochem 59:395-414. doi:10. 1146/annurev.bi.59.070190.002143
8. Rafferty MJ, Bradford AM, Bowie JH, Wallace JC, Tyler MJ (1993) Peptides from Australian frogs. The structure of the dynastins from the Banjo frogs Limnodynastes interioris, Limnodynastes dumerilii and Limndodynastes terraereginae. Aust J Chem 46:833-842
9. Simmaco M, Mignogna G, Barra D (1998) Antimicrobial peptides from amphibian skin: what do they tell us? Biopolymers 47(6):435-450. doi:10.1002/(SICI)1097-0282, (1998) 47:6<435::AID-BIP3>3.0.CO;2-8
10. Simmaco M, Mignogna G, Barra D, Bossa F (1994) Antimicrobial peptides from skin secretions of Rana esculenta. Molecular cloning of cDNAs encoding esculentin and brevinins and isolation of new active peptides. J Biol Chem 269(16):11956-11961
11. Chen T, Farragher S, Bjourson AJ, Orr DF, Rao P, Shaw C (2003) Granular gland transcriptomes in stimulated amphibian skin secretions. Biochem J 371(Pt 1):125-130. doi:10.1042/BJ20021343
12. Mechkarska M, Ojo OO, Meetani MA, Coquet L, Jouenne T, Abdel-Wahab YH, Flatt PR, King JD, Conlon JM (2011) Peptidomic analysis of skin secretions from the bullfrog Lithobates catesbeianus (Ranidae) identifies multiple peptides with potent insulin-releasing activity. Peptides 32(2):203-208. doi:10.1016/j. peptides.2010.11.002
13. Marenah L, Flatt PR, Orr DF, McClean S, Shaw C, Abdel-Wahab YH (2004) Brevinin-1 and multiple insulin-releasing peptides in the skin of the frog Rana palustris. J Endocrinol 181 (2):347-354
14. Basir YJ, Knoop FC, Dulka J, Conlon JM (2000) Multiple antimicrobial peptides and peptides related to bradykinin and neuromedin N isolated from skin secretions of the pickerel frog, Rana palustris. Biochim Biophys Acta 1543(1):95-105
15. Conlon JM (2008) Reflections on a systematic nomenclature for antimicrobial peptides from the skins of frogs of the family Ranidae. Peptides 29(10):1815-1819. doi:10.1016/j.peptides. 2008.05.029
16. Thomas P, Kumar TV, Reshmy V, Kumar KS, George S (2012) A mini review on the antimicrobial peptides isolated from the genus Hylarana (Amphibia: Anura) with a proposed nomenclature for amphibian skin peptides. Mol Biol Rep 39(6):6943-6947. doi:10.1007/ s11033-012-1521-3
17. Morikawa N, Hagiwara K, Nakajima T (1992) Brevinin-1 and -2, unique antimicrobial peptides from the skin of the frog, Rana brevipoda porsa. Biochem Biophys Res Commun 189(1):184-190
18. Novkovic M, Simunic J, Bojovic V, Tossi A, Juretic D (2012) DADP: the database of anuran defense peptides. Bioinformatics 28(10):1406-1407. doi:10.1093/bioinformatics/bts141
19. Mashreghi M, Rezazade Bazaz M, Mahdavi Shahri N, Asoodeh A, Mashreghi M, Behnam Rassouli M, Golmohammadzadeh S (2013) Topical effects of frog "Rana ridibunda" skin secretions on wound healing and reduction of wound microbial load. J Ethnopharmacol 145 (3):793-797. doi:10.1016/j.jep.2012.12.016
20. Asoodeh A, Zardini HZ, Chamani J (2012) Identification and characterization of two novel antimicrobial peptides, temporin-Ra and temporin-Rb, from skin secretions of the marsh frog (Rana ridibunda). J Pept Sci: Off Publ Eur Pept Soc 18(1):10-16. doi:10.1002/psc.1409
21. Clark DP, Durell S, Maloy WL, Zasloff M (1994) Ranalexin. A novel antimicrobial peptide from bullfrog (Rana catesbeiana) skin, structurally related to the bacterial antibiotic, polymyxin. J Biol Chem 269(14):10849-10855
22. Conlon JM, Sonnevend A, Jouenne T, Coquet L, Cosquer D, Vaudry H, Iwamuro S (2005) A family of acyclic brevinin-1 peptides from the skin of the Ryukyu brown frog Rana okinavana. Peptides 26(2):185-190. doi:10.1016/j.peptides.2004. 08.008
23. Conlon JM, Abraham B, Sonnevend A, Jouenne T, Cosette P, Leprince J, Vaudry H, Bevier CR (2005) Purification and characterization of antimicrobial peptides from the skin secretions of the carpenter frog Rana virgatipes (Ranidae, Aquarana). Regul Pept 131(1-3):38-45. doi:10.1016/j.regpep.2005.06.003
24. Conlon JM, Kolodziejek J, Nowotny N (2004) Antimicrobial peptides from ranid frogs: taxonomic and phylogenetic markers and a potential source of new therapeutic agents. Biochim Biophys Acta 1696(1):1-14
25. Suh JY, Lee KH, Chi SW, Hong SY, Choi BW, Moon HM, Choi BS (1996) Unusually stable helical kink in the antimicrobial peptide-a derivative of gaegurin. FEBS Lett 392(3):309-312
26. Kwon MY, Hong SY, Lee KH (1998) Structure-activity analysis of brevinin 1E amide, an antimicrobial peptide from Rana esculenta. Biochim Biophys Acta 1387(1-2):239-248
27. Wade D, Boman A, Wahlin B, Drain CM, Andreu D, Boman HG, Merrifield RB (1990) All-D amino acid-containing channel-forming antibiotic peptides. Proc Natl Acad Sci U S A 87 (12):4761-4765
28. Chan DI, Prenner EJ, Vogel HJ (2006) Tryptophan- and arginine-rich antimicrobial peptides: structures and mechanisms of action. Biochim Biophys Acta 1758(9):1184-1202. doi:10.1016/ j.bbamem.2006.04.006
29. Shai Y (1999) Mechanism of the binding, insertion and destabilization of phospholipid bilayer membranes by alpha-helical antimicrobial and cell non-selective membrane-lytic peptides. Biochim Biophys Acta 1462(1-2):55-70
30. Nicolas P, Vanhoye D, Amiche M (2003) Molecular strategies in biological evolution of antimicrobial peptides. Peptides 24(11):1669-1680. doi:10.1016/j.peptides.2003.08.017
31. Tazato S, Conlon JM, Iwamuro S (2010) Cloning and expression of genes enocoding antimicrobial peptides and bradykinin from the skin and brain of Oki Tago's brown frog, Rana tagoi okiensis. Peptides 31(8):1480-1487. doi:10.1016/j.peptides.2010.04.031
32. Chen T, Li L, Zhou M, Rao P, Walker B, Shaw C (2006) Amphibian skin peptides and their corresponding cDNAs from single lyophilized secretion samples: identification of novel brevinins from three species of Chinese frogs. Peptides 27(1):42-48. doi:10.1016/j.peptides. 2005.06.024
33. Wang H, Ran R, Yu H, Yu Z, Hu Y, Zheng H, Wang D, Yang F, Liu R, Liu J (2012) Identification and characterization of antimicrobial peptides from skin of Amolops ricketti (Anura: Ranidae). Peptides 33(1):27-34. doi:10.1016/j. peptides.2011.10.030
34. Ohnuma A, Conlon JM, Iwamuro S (2010) Differential expression of genes encoding preprobrevinin-2, prepropalustrin-2, and preproranatuerin-2 in developing larvae and adult tissues of the mountain brown frog Rana ornativentris. Comp Biochem Physiol Toxicol Pharmacol CBP 151(1):122-130. doi:10.1016/j.cbpc.2009.09.004
35. Li Y (2009) Carrier proteins for fusion expression of antimicrobial peptides in Escherichia coli. Biotechnol Appl Biochem 54(1):1-9. doi:10.1042/BA20090087
36. Ueberbacher R, Rodler A, Hahn R, Jungbauer A (2010) Hydrophobic interaction chromatography of proteins: thermodynamic analysis of conformational changes. J Chromatogr A 1217 (2):184-190. doi:10.1016/j.chroma.2009.05.033
37. Cheng X, Lu W, Zhang S, Cao P (2010) Expression and purification of antimicrobial peptide CM4 by Npro fusion technology in E. coli. Amino Acids 39(5):1545-1552. doi:10.1007/ s00726-010-0625-0
38. Ke T, Liang S, Huang J, Mao H, Chen J, Dong C, Huang J, Liu S, Kang J, Liu D, Ma X (2012) A novel PCR-based method for high throughput prokaryotic expression of antimicrobial peptide genes. BMC Biotechnol 12:10. doi:10.1186/1472-6750-12-10
39. Mehrnejad F, Naderi-Manesh H, Ranjbar B, Maroufi B, Asoodeh A, Doustdar F (2008) PCR-based gene synthesis, molecular cloning, high level expression, purification, and characterization of novel antimicrobial peptide, brevinin-2R, in Escherichia coli. Appl Biochem Biotechnol 149(2):109-118. doi:10.1007/s12010-007-8024-z
40. Zhou QF, Li MY, Li CW (2009) Cloning and expression of a novel insulin-releasing peptide, brevinin-2GU from Escherichia coli. J Biosci Bioeng 107(4):460-463. doi:10.1016/j.jbiosc. 2008.12.011
41. Yasin B, Pang M, Turner JS, Cho Y, Dinh NN, Waring AJ, Lehrer RI, Wagar EA (2000) Evaluation of the inactivation of infectious Herpes simplex virus by host-defense peptides. Eur J Clin Microbiol Infect Dis 19(3):187-194
42. Kumari VK, Nagaraj R (2001) Structure-function studies on the amphibian peptide brevinin 1E: translocating the cationic segment from the C-terminal end to a central position favors selective antibacterial activity. J Pept Res: Off J Am Pept Soc 58(5):433-441
43. Conlon JM, Ahmed E, Condamine E (2009) Antimicrobial properties of brevinin-2-related peptide and its analogs: efficacy against multidrug-resistant Acinetobacter baumannii. Chem Biol Drug Des 74(5):488-493. doi:10.1111/j.1747- 0285.2009.00882.x
44. Popovic S, Urban E, Lukic M, Conlon JM (2012) Peptides with antimicrobial and antiinflammatory activities that have therapeutic potential for treatment of acne vulgaris. Peptides 34(2):275-282. doi:10.1016/j.peptides.2012.02.010
45. Ghavami S, Asoodeh A, Klonisch T, Halayko AJ, Kadkhoda K, Kroczak TJ, Gibson SB, Booy EP, Naderi-Manesh H, Los M (2008) Brevinin-2R(1) semi-selectively kills cancer cells by a distinct mechanism, which involves the lysosomal-mitochondrial death pathway. J Cell Mol Med 12(3):1005-1022. doi:10.1111/j.1582-4934.2008.00129.x
46. Papo N, Shai Y (2005) Host defense peptides as new weapons in cancer treatment. Cell Mol Life Sci CMLS 62(7-8):784-790. doi:10.1007/s00018-005-4560-2
47. Utsugi T, Schroit AJ, Connor J, Bucana CD, Fidler IJ (1991) Elevated expression of phosphatidylserine in the outer membrane leaflet of human tumor cells and recognition by activated human blood monocytes. Cancer Res 51(11):3062-3066
48. Zwaal RF, Schroit AJ (1997) Pathophysiologic implications of membrane phospholipid asymmetry in blood cells. Blood 89(4):1121-1132
49. Conlon JM, Power GJ, Abdel-Wahab YH, Flatt PR, Jiansheng H, Coquet L, Leprince J, Jouenne T, Vaudry H (2008) A potent, non-toxic insulin-releasing peptide isolated from an extract of the skin of the Asian frog, Hylarana guntheri (Anura:Ranidae). Regul Pept 151 (1-3):153-159. doi:10.1016/j.regpep. 2008.04.002
50. Abdel-Wahab YH, Patterson S, Flatt PR, Conlon JM (2010) Brevinin-2-related peptide and its [D4K] analogue stimulate insulin release in vitro and improve glucose tolerance in mice fed a high fat diet. Horm Metab Res 42(9):652-656. doi:10.1055/s-0030-1254126
51. Marenah L, Flatt PR, Orr DF, Shaw C, Abdel-Wahab YH (2006) Skin secretions of Rana saharica frogs reveal antimicrobial peptides esculentins-1 and -1B and brevinins-1E and -2EC with novel insulin releasing activity. J Endocrinol 188(1):1-9. doi:10.1677/joe.1.06293
52. Kim JH, Lee JO, Jung JH, Lee SK, You GY, Park SH, Kim HS (2010) Gaegurin-6 stimulates insulin secretion through calcium influx in pancreatic beta Rin5mf cells. Regul Pept 159 (1-3):123-128. doi:10.1016/j.regpep.2009.07. 014
53. Abdel-Wahab YH, Power GJ, Flatt PR, Woodhams DC, Rollins-Smith LA, Conlon JM (2008) A peptide of the phylloseptin family from the skin of the frog Hylomantis lemur (Phyllomedusinae) with potent in vitro and in vivo insulin-releasing activity. Peptides 29 (12):2136-2143. doi:10.1016/j.peptides. 2008.09.006
54. Veerapandian M, Yun K (2011) Functionalization of biomolecules on nanoparticles: specialized for antibacterial applications. Appl Microbiol Biotechnol 90(5):1655-1667. doi:10.1007/ s00253-011-3291-6
55. Mohan R, Shanmugharaj AM, Sung Hun R (2011) An efficient growth of silver and copper nanoparticles on multiwalled carbon nanotube with enhanced antimicrobial activity. J Biomed Mater Res B Appl Biomater 96(1):119-126. doi:10.1002/jbm.b.31747
56. Liu L, Xu K, Wang H, Tan PK, Fan W, Venkatraman SS, Li L, Yang YY (2009) Self-assembled cationic peptide nanoparticles as an efficient antimicrobial agent. Nat Nanotechnol 4(7):457-463. doi:10.1038/nnano.2009.153
57. Kumar A, Ma H, Zhang X, Huang K, Jin S, Liu J, Wei T, Cao W, Zou G, Liang XJ (2012) Gold nanoparticles functionalized with therapeutic and targeted peptides for cancer treatment. Biomaterials 33(4):1180-1189. doi:10.1016/j.biomaterials.2011.10.058
58. Lia T, Heab X, Wang Z (2012) The application of peptide functionalized gold nanoparticles. In: Hepel M, Zhong C (eds) Functional nanoparticles for bioanalysis, nanomedicine, and bioelectronic devices, vol 2. American Chemical Society, Washington, DC, pp 55-68. doi:10.1021/bk-2012-1113
59. de la Fuente JM, Berry CC (2005) Tat peptide as an efficient molecule to translocate gold nanoparticles into the cell nucleus. Bioconjug Chem 16(5):1176-1180. doi:10.1021/bc050033+
60. Goraya J, Wang Y, Li Z, O'Flaherty M, Knoop FC, Platz JE, Conlon JM (2000) Peptides with antimicrobial activity from four different families isolated from the skins of the North American frogs Rana luteiventris, Rana berlandieri and Rana pipiens. Eur J Biochem/ FEBS 267(3):894-900
61. Conlon JM, Sonnevend A, Patel M, Al-Dhaheri K, Nielsen PF, Kolodziejek J, Nowotny N, Iwamuro S, Pal T (2004) A family of brevinin-2 peptides with potent activity against Pseudomonas aeruginosa from the skin of the Hokkaido frog, Rana pirica. Regul Pept 118 (3):135-141. doi:10.1016/j.regpep.2003.12.003