메뉴 건너뛰기




Volumn 56, Issue 6, 2012, Pages 3004-3010

Effects of dimerization on the structure and biological activity of antimicrobial peptide Ctx-Ha

Author keywords

[No Author keywords available]

Indexed keywords

CARBOXYFLUORESCEIN; CTX HA; POLYPEPTIDE ANTIBIOTIC AGENT; SPHINGOMYELIN; UNCLASSIFIED DRUG;

EID: 84861170375     PISSN: 00664804     EISSN: 10986596     Source Type: Journal    
DOI: 10.1128/AAC.06262-11     Document Type: Article
Times cited : (59)

References (45)
  • 1
    • 70349650567 scopus 로고    scopus 로고
    • Activity of antimicrobial peptides in the presence of polysaccharides produced by pulmonary pathogens
    • Benincasa M, et al. 2009. Activity of antimicrobial peptides in the presence of polysaccharides produced by pulmonary pathogens. J. Pept. Sci. 9:595-600.
    • (2009) J. Pept. Sci. , vol.9 , pp. 595-600
    • Benincasa, M.1
  • 2
    • 33645739372 scopus 로고    scopus 로고
    • Model peptides mimic the structure and function of the N-terminus of the pore-forming toxin sticholysin. II
    • Casallanovo F, et al. 2006. Model peptides mimic the structure and function of the N-terminus of the pore-forming toxin sticholysin. II. Biopolymers 84:169-180.
    • (2006) Biopolymers , vol.84 , pp. 169-180
    • Casallanovo, F.1
  • 3
    • 58149488747 scopus 로고    scopus 로고
    • Hylin a1, the first cytolytic peptide isolated from the arboreal South American frog Hypsiboas albopunctatus ("spotted treefrog")
    • Castro MS, et al. 2009. Hylin a1, the first cytolytic peptide isolated from the arboreal South American frog Hypsiboas albopunctatus ("spotted treefrog"). Peptides 30:291-296.
    • (2009) Peptides , vol.30 , pp. 291-296
    • Castro, M.S.1
  • 4
    • 85088716273 scopus 로고    scopus 로고
    • Mechanism of action and relationship between structure and biological activity of Ctx-Ha, a new ceratotoxin-like peptide from Hypsiboas albopunctatus
    • Cespedes GF, et al. Mechanism of action and relationship between structure and biological activity of Ctx-Ha, a new ceratotoxin-like peptide from Hypsiboas albopunctatus. Protein Pept. Lett. 19:595-602.
    • Protein Pept. Lett. , vol.19 , pp. 595-602
    • Cespedes, G.F.1
  • 5
    • 16844373772 scopus 로고    scopus 로고
    • Rational design of alpha-helical antimicrobial peptides with enhanced activities and specificity/therapeutic index
    • Chen YX, et al. 2005. Rational design of alpha-helical antimicrobial peptides with enhanced activities and specificity/therapeutic index. J. Biol. Chem. 280:12316-12329.
    • (2005) J. Biol. Chem. , vol.280 , pp. 12316-12329
    • Chen, Y.X.1
  • 6
    • 34247153326 scopus 로고    scopus 로고
    • Role of peptide hydrophobicity in the mechanism of action of alpha-helical antimicrobial peptides
    • Chen YX, et al. 2007. Role of peptide hydrophobicity in the mechanism of action of alpha-helical antimicrobial peptides. Antimicrob. Agents Chemother. 51:1398-1406.
    • (2007) Antimicrob. Agents Chemother. , vol.51 , pp. 1398-1406
    • Chen, Y.X.1
  • 7
    • 36048975351 scopus 로고    scopus 로고
    • Correlations between differences in amino-terminal sequences and different hemolytic activity of sticholysins
    • DOI 10.1016/j.toxicon.2007.07.013, PII S0041010107002863
    • Cilli EM, et al. 2007. Correlations between differences in amino-terminal sequences and different hemolytic activity of sticholysins. Toxicon 50:1201-1204. (Pubitemid 350087175)
    • (2007) Toxicon , vol.50 , Issue.8 , pp. 1201-1204
    • Cilli, E.M.1    Pigossi, F.T.2    Crusca Jr., E.3    Ros, U.4    Martinez, D.5    Lanio, M.E.6    Alvarez, C.7    Schreier, S.8
  • 8
    • 84861172494 scopus 로고    scopus 로고
    • Performance standards for antimicrobial susceptibility testing
    • Clinical and Laboratory Standards Institute. 6th ed. Document M7-A6. Clinical and Laboratory Standards Institute, Wayne, PA
    • Clinical and Laboratory Standards Institute. 2006. Methods for dilution antimicrobial susceptibility tests for bacteria that grow aerobically; approved standards, 6th ed. Document M7-A6. Performance standards for antimicrobial susceptibility testing. Clinical and Laboratory Standards Institute, Wayne, PA.
    • (2006) Methods for Dilution Antimicrobial Susceptibility Tests for Bacteria That Grow Aerobically; Approved Standards
  • 9
    • 84861172493 scopus 로고    scopus 로고
    • Performance standards for antimicrobial susceptibility testing
    • Clinical and Laboratory Standards Institute. 6th ed. Document M27-A2. Clinical and Laboratory Standards Institute, Wayne, PA
    • Clinical and Laboratory Standards Institute. 2006. Methods for dilution antimicrobial susceptibility tests for yeast; approved standards, 6th ed. Document M27-A2. Performance standards for antimicrobial susceptibility testing. Clinical and Laboratory Standards Institute, Wayne, PA.
    • (2006) Methods for Dilution Antimicrobial Susceptibility Tests for Yeast; Approved Standards
  • 10
    • 79959776511 scopus 로고    scopus 로고
    • Influence of N-terminus modifications on the biological activity, membrane interaction, and secondary structure of the antimicrobial peptide Hylin-a1
    • Crusca E, et al. 2011. Influence of N-terminus modifications on the biological activity, membrane interaction, and secondary structure of the antimicrobial peptide Hylin-a1. Biopolymers 96:41-48.
    • (2011) Biopolymers , vol.96 , pp. 41-48
    • Crusca, E.1
  • 11
    • 0037457904 scopus 로고    scopus 로고
    • Enhanced membrane permeabilization and antibacterial activity of a disulfide-dimerized magainin analogue
    • DOI 10.1021/bi026328h
    • Dempsey CE, Ueno S, Avison MB. 2003. Enhanced membrane permeabilization and antibacterial activity of a disulfide-dimerized magainin analogue. Biochemistry 42:402-409. (Pubitemid 36105758)
    • (2003) Biochemistry , vol.42 , Issue.2 , pp. 402-409
    • Dempsey, C.E.1    Ueno, S.2    Avison, M.B.3
  • 12
    • 33645767676 scopus 로고    scopus 로고
    • Adding selectivity to antimicrobial peptides: Rational design of a multidomain peptide against Pseudomonas spp
    • Eckert R, et al. 2006. Adding selectivity to antimicrobial peptides: rational design of a multidomain peptide against Pseudomonas spp. Antimicrob. Agents Chemother. 50:1480-1488.
    • (2006) Antimicrob. Agents Chemother. , vol.50 , pp. 1480-1488
    • Eckert, R.1
  • 15
    • 77649237880 scopus 로고    scopus 로고
    • Antimicrobial peptides: General overview and clinical implications in human health and disease
    • Guani-Guerra E, Santos-Mendoza T, Lugo-Reyes SO, Teran LM. 2010. Antimicrobial peptides: general overview and clinical implications in human health and disease. Clin. Immunol. 135:1-11.
    • (2010) Clin. Immunol. , vol.135 , pp. 1-11
    • Guani-Guerra, E.1    Santos-Mendoza, T.2    Lugo-Reyes, S.O.3    Teran, L.M.4
  • 16
    • 0035115807 scopus 로고    scopus 로고
    • Effects of peptide dimerization on pore formation: Antiparallel disulfide-dimerized magainin 2 analogue
    • Hara T, et al. 2001. Effects of peptide dimerization on pore formation: antiparallel disulfide-dimerized magainin 2 analogue. Biopolymers 58:437-446. (Pubitemid 32187679)
    • (2001) Biopolymers , vol.58 , Issue.4 , pp. 437-446
    • Hara, T.1    Kodama, H.2    Kondo, M.3    Wakamatsu, K.4    Takeda, A.5    Tachi, T.6    Matsuzaki, K.7
  • 17
    • 4444246183 scopus 로고    scopus 로고
    • Increased diversity of intestinal antimicrobial peptides by covalent dimer formation
    • DOI 10.1038/ni1094
    • Hornef MW, Putsep K, Karlsson J, Refai E, Andersson M. 2004. Increased diversity of intestinal antimicrobial peptides by covalent dimer formation. Nat. Immunol. 5:836-843. (Pubitemid 39172977)
    • (2004) Nature Immunology , vol.5 , Issue.8 , pp. 836-843
    • Hornef, M.W.1    Putsep, K.2    Karlsson, J.3    Refai, E.4    Andersson, M.5
  • 18
    • 79953148897 scopus 로고    scopus 로고
    • Alpha-helical cationic antimicrobial peptides: Relationships of structure and function
    • Huang Y, Huang J, Chen Y. 2010. Alpha-helical cationic antimicrobial peptides: relationships of structure and function. Protein Cell 1:143-152.
    • (2010) Protein Cell , vol.1 , pp. 143-152
    • Huang, Y.1    Huang, J.2    Chen, Y.3
  • 19
    • 0043245859 scopus 로고    scopus 로고
    • Peptides with anticancer use or potential
    • Janin YL. 2003. Peptides with anticancer use or potential. Amino Acids 25:1-40. (Pubitemid 36934517)
    • (2003) Amino Acids , vol.25 , Issue.1 , pp. 1-40
    • Janin, Y.L.1
  • 20
    • 79952614254 scopus 로고    scopus 로고
    • Rational design of alpha-helical antimicrobial peptides to target gram-negative pathogens, Acinetobacter baumannii and Pseudomonas aeruginosa: Utilization of charge, 'specificity determinants', total hydrophobicity, hydrophobe type and location as design parameters to improve the therapeutic ratio
    • Jiang Z, Vasil AI, Gera L, Vasil ML, Hodges RS. 2011. Rational design of alpha-helical antimicrobial peptides to target gram-negative pathogens, Acinetobacter baumannii and Pseudomonas aeruginosa: utilization of charge, 'specificity determinants', total hydrophobicity, hydrophobe type and location as design parameters to improve the therapeutic ratio. Chem. Biol. Drug Des. 77:225-240.
    • (2011) Chem. Biol. Drug Des. , vol.77 , pp. 225-240
    • Jiang, Z.1    Vasil, A.I.2    Gera, L.3    Vasil, M.L.4    Hodges, R.S.5
  • 22
    • 0034855781 scopus 로고    scopus 로고
    • Evaluation of the trifluoromethanosulfonic acid/trifluoroacetic acid/thioanisole cleavage procedure for application in solid-phase peptide synthesis
    • DOI 10.1248/cpb.49.1089
    • Jubilut GN, et al. 2001. Evaluation of the trifluoromethanosulfonic acid/trifluoroacetic acid/thioanisole cleavage procedure for application in solid-phase peptide synthesis. Chem. Pharm. Bull. 49:1089-1092. (Pubitemid 32847513)
    • (2001) Chemical and Pharmaceutical Bulletin , vol.49 , Issue.9 , pp. 1089-1092
    • Jubilut, G.N.1    Cilli, E.M.2    Tominaga, M.3    Miranda, A.4    Okada, Y.5    Nakaie, C.R.6
  • 23
    • 47249135720 scopus 로고    scopus 로고
    • Salt-resistant homodimeric bactenecin, a cathelicidin-derived antimicrobial peptide
    • DOI 10.1111/j.1742-4658.2008.06536.x
    • Lee JY, et al. 2008. Salt-resistant homodimeric bactenecin, a cathelicidin-derived antimicrobial peptide. FEBS J. 275:3911-3920. (Pubitemid 351990953)
    • (2008) FEBS Journal , vol.275 , Issue.15 , pp. 3911-3920
    • Lee, J.Y.1    Yang, S.-T.2    Lee, S.K.3    Jung, H.H.4    Shin, S.Y.5    Hahm, K.-S.6    Kim, J.I.7
  • 24
    • 78751577584 scopus 로고    scopus 로고
    • Anti-proliferative and cytotoxic activity of pentadactylin isolated from Leptodactylus labyrinthicus on melanoma cells
    • Libério MS, et al. 2011. Anti-proliferative and cytotoxic activity of pentadactylin isolated from Leptodactylus labyrinthicus on melanoma cells. Amino Acids 40:51-59.
    • (2011) Amino Acids , vol.40 , pp. 51-59
    • Libério, M.S.1
  • 25
    • 79951556373 scopus 로고    scopus 로고
    • Multivalent antimicrobial peptides as therapeutics: Design principles and structural diversities
    • Liu S, Zhou L, Lakshminarayanan R, Beuerman R. 2010. Multivalent antimicrobial peptides as therapeutics: design principles and structural diversities. Int. J. Pept. Protein Res. 16:199-213.
    • (2010) Int. J. Pept. Protein Res. , vol.16 , pp. 199-213
    • Liu, S.1    Zhou, L.2    Lakshminarayanan, R.3    Beuerman, R.4
  • 27
    • 67649256037 scopus 로고    scopus 로고
    • Control of cell selectivity of antimicrobial peptides
    • Matsuzaki K. 2009. Control of cell selectivity of antimicrobial peptides. Biochim. Biophys. Acta 1788:1687-1692.
    • (2009) Biochim. Biophys. Acta , vol.1788 , pp. 1687-1692
    • Matsuzaki, K.1
  • 28
    • 60749118913 scopus 로고    scopus 로고
    • Antimicrobial peptides: Linking partition, activity and high membrane-bound concentrations
    • Melo MN, Ferre R, Castanho MARB. 2009. Antimicrobial peptides: linking partition, activity and high membrane-bound concentrations. Nat. Rev. Microbiol. 7:245-250.
    • (2009) Nat. Rev. Microbiol. , vol.7 , pp. 245-250
    • Melo, M.N.1    Ferre, R.2    Castanho, M.A.R.B.3
  • 29
    • 77951207345 scopus 로고    scopus 로고
    • Effects of reducing beta-lactam antibiotic pressure on intestinal colonization of antibiotic-resistant gram-negative bacteria
    • Nijssen S, et al. 2010. Effects of reducing beta-lactam antibiotic pressure on intestinal colonization of antibiotic-resistant gram-negative bacteria. Intensive Care Med. 36:512-519.
    • (2010) Intensive Care Med. , vol.36 , pp. 512-519
    • Nijssen, S.1
  • 30
  • 31
    • 77951626660 scopus 로고    scopus 로고
    • A novel tetrabranched antimicrobial peptide that neutralizes bacterial lipopolysaccharide and prevents septic shock in vivo
    • Pini A, et al. 2010. A novel tetrabranched antimicrobial peptide that neutralizes bacterial lipopolysaccharide and prevents septic shock in vivo. FASEB J. 24:1015-1022.
    • (2010) FASEB J. , vol.24 , pp. 1015-1022
    • Pini, A.1
  • 33
    • 52049109183 scopus 로고    scopus 로고
    • Toroidal pores formed by antimicrobial peptides show significant disorder
    • Sengupta D, Leontiadou H, Mark AE, Marrink SJ. 2008. Toroidal pores formed by antimicrobial peptides show significant disorder. Biochim. Biophys. Acta 1778:2308-2317.
    • (2008) Biochim. Biophys. Acta , vol.1778 , pp. 2308-2317
    • Sengupta, D.1    Leontiadou, H.2    Mark, A.E.3    Marrink, S.J.4
  • 34
    • 59749089160 scopus 로고    scopus 로고
    • Evaluation of strategies for improving proteolytic resistance of antimicrobial peptides by using variants of EFK17, an internal segment of LL-37
    • Strömstedt AA, Pasupuleti M, Schmidtchen A, Malmsten M. 2009. Evaluation of strategies for improving proteolytic resistance of antimicrobial peptides by using variants of EFK17, an internal segment of LL-37. Antimicrob. Agents Chemother. 53:593-602.
    • (2009) Antimicrob. Agents Chemother. , vol.53 , pp. 593-602
    • Strömstedt, A.A.1    Pasupuleti, M.2    Schmidtchen, A.3    Malmsten, M.4
  • 35
    • 0001331728 scopus 로고
    • Synthetic peptide vaccine design-synthesis and properties of a high-density multiple antigenic peptide system
    • Tam JP. 1988. Synthetic peptide vaccine design-synthesis and properties of a high-density multiple antigenic peptide system. Proc. Natl. Acad. Sci. U. S. A. 85:5409-5413.
    • (1988) Proc. Natl. Acad. Sci. U. S. A. , vol.85 , pp. 5409-5413
    • Tam, J.P.1
  • 37
    • 79952679401 scopus 로고    scopus 로고
    • Human antimicrobial peptide LL-37 inhibits adhesion of Candida albicans by interacting with yeast cell-wall carbohydrates
    • Tsai PW, Yang CY, Chang HT, Lan CY. 2011. Human antimicrobial peptide LL-37 inhibits adhesion of Candida albicans by interacting with yeast cell-wall carbohydrates. PLoS One 6:e17755.
    • (2011) PLoS One , vol.6
    • Tsai, P.W.1    Yang, C.Y.2    Chang, H.T.3    Lan, C.Y.4
  • 38
    • 77952548132 scopus 로고    scopus 로고
    • Cell selectivity and anti-inflammatory activity of a Leu/Lys-rich alpha-helical model antimicrobial peptide and its diastereomeric peptides
    • Wang P, et al. 2010. Cell selectivity and anti-inflammatory activity of a Leu/Lys-rich alpha-helical model antimicrobial peptide and its diastereomeric peptides. Peptides 31:1251-1261.
    • (2010) Peptides , vol.31 , pp. 1251-1261
    • Wang, P.1
  • 39
    • 35948959330 scopus 로고    scopus 로고
    • Histatin-derived monomeric and dimeric synthetic peptides show-strong bactericidal activity towards multidrug-resistant Staphylococcus aureus in vivo
    • DOI 10.1128/AAC.00196-07
    • Welling MM, Brouwer CP, Wvan't Hof Veerman EC, Amerongen AV. 2007. Histatin-derived monomeric and dimeric synthetic peptides show strong bactericidal activity towards multidrug-resistant Staphylococcus aureus in vivo. Antimicrob. Agents Chemother. 51:3416-3419. (Pubitemid 350067569)
    • (2007) Antimicrobial Agents and Chemotherapy , vol.51 , Issue.9 , pp. 3416-3419
    • Welling, M.M.1    Brouwer, C.P.J.M.2    Van 't, H.W.3    Veerman, E.C.I.4    Nieuw, A.A.V.5
  • 40
    • 58149202358 scopus 로고    scopus 로고
    • Effect of dimerization of a beta-turn antimicrobial peptide, PST13-RK, on antimicrobial activity and mammalian cell toxicity
    • Yang ST, Kim JI, Shin SY. 2009. Effect of dimerization of a beta-turn antimicrobial peptide, PST13-RK, on antimicrobial activity and mammalian cell toxicity. Biotechnol. Lett. 31:233-237.
    • (2009) Biotechnol. Lett. , vol.31 , pp. 233-237
    • Yang, S.T.1    Kim, J.I.2    Shin, S.Y.3
  • 41
    • 11244292022 scopus 로고    scopus 로고
    • Immunocontinuum: Perspectives in antimicrobial peptide mechanisms of action and resistance
    • DOI 10.2174/0929866053405959
    • Yount NY, Yeaman MR. 2005. Immunocontinuum: perspectives in antimicrobial peptide mechanisms of action and resistance. Protein Pept. Lett. 12:49-67. (Pubitemid 40068360)
    • (2005) Protein and Peptide Letters , vol.12 , Issue.1 , pp. 49-67
    • Yount, N.Y.1    Yeaman, M.R.2
  • 42
    • 77954559555 scopus 로고    scopus 로고
    • Hemolytic activity of a bacterial trehalose lipid biosurfactant produced by Rhodococcus sp.: Evidence for a colloidosmotic mechanism
    • Zaragoza A, et al. 2010. Hemolytic activity of a bacterial trehalose lipid biosurfactant produced by Rhodococcus sp.: evidence for a colloidosmotic mechanism. Langmuir 26:8567-8572.
    • (2010) Langmuir , vol.26 , pp. 8567-8572
    • Zaragoza, A.1
  • 43
    • 36949003906 scopus 로고    scopus 로고
    • Cell selectivity of an antimicrobial peptide melittin diastereomer with D-amino acid in the leucine zipper sequence
    • Zhu WL, Nan YH, Hahm KS, Shin SY. 2007. Cell selectivity of an antimicrobial peptide melittin diastereomer with D-amino acid in the leucine zipper sequence. J. Biochem. Mol. Biol. 40:1090-1094.
    • (2007) J. Biochem. Mol. Biol. , vol.40 , pp. 1090-1094
    • Zhu, W.L.1    Nan, Y.H.2    Hahm, K.S.3    Shin, S.Y.4
  • 44
    • 67649234630 scopus 로고    scopus 로고
    • Effects of dimerization of the cell-penetrating peptide Tat analog on antimicrobial activity and mechanism of bactericidal action
    • Zhu WL, Shin SY. 2009. Effects of dimerization of the cell-penetrating peptide Tat analog on antimicrobial activity and mechanism of bactericidal action. J. Pept. Sci. 15:345-352.
    • (2009) J. Pept. Sci. , vol.15 , pp. 345-352
    • Zhu, W.L.1    Shin, S.Y.2
  • 45
    • 58849116845 scopus 로고    scopus 로고
    • Antimicrobial and cytolytic activities and plausible mode of bactericidal action of the cell penetrating peptide penetratin and its Lys-linked two-stranded peptide
    • Zhu WL, Shin SY. 2009. Antimicrobial and cytolytic activities and plausible mode of bactericidal action of the cell penetrating peptide penetratin and its Lys-linked two-stranded peptide. Chem. Biol. Drug Des. 73:209-215.
    • (2009) Chem. Biol. Drug Des. , vol.73 , pp. 209-215
    • Zhu, W.L.1    Shin, S.Y.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.