메뉴 건너뛰기




Volumn 36, Issue 2, 2012, Pages 303-307

Importance of the disulfide bridges in the antibacterial activity of human hepcidin

Author keywords

Antimicrobial peptide; Disulfide bridges; DNA binding; Hepcidin

Indexed keywords

ALANINE; CATHELICIDIN ANTIMICROBIAL PEPTIDE LL 37; CYSTEINE; HEPCIDIN; MAGAININ 2; SYNTHETIC PEPTIDE;

EID: 84864124975     PISSN: 01969781     EISSN: 18735169     Source Type: Journal    
DOI: 10.1016/j.peptides.2012.06.001     Document Type: Article
Times cited : (60)

References (27)
  • 1
    • 50049127533 scopus 로고    scopus 로고
    • Use of a real-time polymerase chain reaction thermocycler to study bacterial cell permeabilization by antimicrobial peptides
    • C. Bourbon, C. Bry, C. Roggemans, C. Soulard, C. Thizon, and B. Garbay Use of a real-time polymerase chain reaction thermocycler to study bacterial cell permeabilization by antimicrobial peptides Anal Biochem 381 2008 279 281
    • (2008) Anal Biochem , vol.381 , pp. 279-281
    • Bourbon, C.1    Bry, C.2    Roggemans, C.3    Soulard, C.4    Thizon, C.5    Garbay, B.6
  • 2
    • 10344240423 scopus 로고    scopus 로고
    • Structure-activity relationships in defensin dimers: A novel link between beta-defensin tertiary structure and antimicrobial activity
    • D.J. Campopiano, D.J. Clarke, N.C. Polfer, P.E. Barran, R.J. Langley, and J.R. Govan Structure-activity relationships in defensin dimers: a novel link between beta-defensin tertiary structure and antimicrobial activity J Biol Chem 279 2004 48671 48679
    • (2004) J Biol Chem , vol.279 , pp. 48671-48679
    • Campopiano, D.J.1    Clarke, D.J.2    Polfer, N.C.3    Barran, P.E.4    Langley, R.J.5    Govan, J.R.6
  • 3
    • 79953061479 scopus 로고    scopus 로고
    • Understanding the structure/activity relationships of the iron regulatory peptide hepcidin
    • R.J. Clark, C.C. Tan, G.C. Preza, E. Nemeth, T. Ganz, and D.J. Craik Understanding the structure/activity relationships of the iron regulatory peptide hepcidin Chem Biol 18 2011 336 343
    • (2011) Chem Biol , vol.18 , pp. 336-343
    • Clark, R.J.1    Tan, C.C.2    Preza, G.C.3    Nemeth, E.4    Ganz, T.5    Craik, D.J.6
  • 4
    • 33845699790 scopus 로고    scopus 로고
    • Antimicrobial and host-defense peptides as new anti-infective therapeutic strategies
    • R.E. Hancock, and H.G. Sahl Antimicrobial and host-defense peptides as new anti-infective therapeutic strategies Nat Biotechnol 24 2006 1551 1557
    • (2006) Nat Biotechnol , vol.24 , pp. 1551-1557
    • Hancock, R.E.1    Sahl, H.G.2
  • 5
    • 73049108637 scopus 로고    scopus 로고
    • Structure-activity relationship of human liver-expressed antimicrobial peptide 2
    • A. Hocquellet, B. Odaert, C. Cabanne, A. Noubhani, W. Dieryck, and G. Joucla Structure-activity relationship of human liver-expressed antimicrobial peptide 2 Peptides 31 2010 58 66
    • (2010) Peptides , vol.31 , pp. 58-66
    • Hocquellet, A.1    Odaert, B.2    Cabanne, C.3    Noubhani, A.4    Dieryck, W.5    Joucla, G.6
  • 8
    • 0032488904 scopus 로고    scopus 로고
    • Conformation-dependent antibacterial activity of the naturally occurring human peptide LL-37
    • J. Johansson, G.H. Gudmundsson, M.E. Rottenberg, K.D. Berndt, and B. Agerberth Conformation-dependent antibacterial activity of the naturally occurring human peptide LL-37 J Biol Chem 273 1998 3718 3724
    • (1998) J Biol Chem , vol.273 , pp. 3718-3724
    • Johansson, J.1    Gudmundsson, G.H.2    Rottenberg, M.E.3    Berndt, K.D.4    Agerberth, B.5
  • 9
    • 22244480342 scopus 로고    scopus 로고
    • Structure-activity relation of human beta-defensin 3: Influence of disulfide bonds and cysteine substitution on antimicrobial activity and cytotoxicity
    • E. Klüver, S. Schulz-Maronde, S. Scheid, B. Meyer, W.G. Forssmann, and K. Adermann Structure-activity relation of human beta-defensin 3: influence of disulfide bonds and cysteine substitution on antimicrobial activity and cytotoxicity Biochemistry 44 2005 9804 9816
    • (2005) Biochemistry , vol.44 , pp. 9804-9816
    • Klüver, E.1    Schulz-Maronde, S.2    Scheid, S.3    Meyer, B.4    Forssmann, W.G.5    Adermann, K.6
  • 10
  • 11
    • 12244313876 scopus 로고    scopus 로고
    • Isolation and biochemical characterization of LEAP-2, a novel blood peptide expressed in the liver
    • A. Krause, R. Sillard, B. Kleemeier, E. Klüver, E. Maronde, and J.R. Conejo-García Isolation and biochemical characterization of LEAP-2, a novel blood peptide expressed in the liver Protein Sci 12 2003 143 152
    • (2003) Protein Sci , vol.12 , pp. 143-152
    • Krause, A.1    Sillard, R.2    Kleemeier, B.3    Klüver, E.4    Maronde, E.5    Conejo-García, J.R.6
  • 12
    • 0042072743 scopus 로고    scopus 로고
    • Single disulfide and linear analogues corresponding to the carboxy-terminal segment of bovine beta-defensin-2: Effects of introducing the beta-hairpin nucleating sequence d-pro-gly on antibacterial activity and biophysical properties
    • V. Krishnakumari, A. Sharadadevi, S. Singh, and R. Nagaraj Single disulfide and linear analogues corresponding to the carboxy-terminal segment of bovine beta-defensin-2: effects of introducing the beta-hairpin nucleating sequence d-pro-gly on antibacterial activity and biophysical properties Biochemistry 42 2003 9307 9315
    • (2003) Biochemistry , vol.42 , pp. 9307-9315
    • Krishnakumari, V.1    Sharadadevi, A.2    Singh, S.3    Nagaraj, R.4
  • 13
    • 0036171208 scopus 로고    scopus 로고
    • Antibacterial activities and conformations of bovine beta-defensin BNBD-12 and analogs: Structural and disulfide bridge requirements for activity
    • M. Mandal, M.V. Jagannadham, and R. Nagaraj Antibacterial activities and conformations of bovine beta-defensin BNBD-12 and analogs: structural and disulfide bridge requirements for activity Peptides 23 2002 413 418
    • (2002) Peptides , vol.23 , pp. 413-418
    • Mandal, M.1    Jagannadham, M.V.2    Nagaraj, R.3
  • 14
    • 0030738014 scopus 로고    scopus 로고
    • Interactions of an antimicrobial peptide, magainin 2, with outer and inner membranes of Gram-negative bacteria
    • K. Matsuzaki, K.I. Sugishita, M. Harada, N. Fujii, and K. Miyajima Interactions of an antimicrobial peptide, magainin 2, with outer and inner membranes of Gram-negative bacteria Biochim Biophys Acta 1327 1997 119 130
    • (1997) Biochim Biophys Acta , vol.1327 , pp. 119-130
    • Matsuzaki, K.1    Sugishita, K.I.2    Harada, M.3    Fujii, N.4    Miyajima, K.5
  • 15
    • 10844258104 scopus 로고    scopus 로고
    • Hepcidin regulates cellular iron efflux by binding to ferroportin and inducing its internalization
    • E. Nemeth, M.S. Tuttle, J. Powelson, M.B. Vaughn, A. Donovan, and D.M. Ward Hepcidin regulates cellular iron efflux by binding to ferroportin and inducing its internalization Science 306 2004 2090 2093
    • (2004) Science , vol.306 , pp. 2090-2093
    • Nemeth, E.1    Tuttle, M.S.2    Powelson, J.3    Vaughn, M.B.4    Donovan, A.5    Ward, D.M.6
  • 16
    • 30144432585 scopus 로고    scopus 로고
    • The N-terminus of hepcidin is essential for its interaction with ferroportin: Structure-function study
    • E. Nemeth, G.C. Preza, C.L. Jung, J. Kaplan, A.J. Waring, and T. Ganz The N-terminus of hepcidin is essential for its interaction with ferroportin: structure-function study Blood 107 2006 328 333
    • (2006) Blood , vol.107 , pp. 328-333
    • Nemeth, E.1    Preza, G.C.2    Jung, C.L.3    Kaplan, J.4    Waring, A.J.5    Ganz, T.6
  • 17
    • 0033178532 scopus 로고    scopus 로고
    • Structure and organization of the human antimicrobial peptide LL-37 in phospholipids membranes: Relevance to the molecular basis for its non-cell-selective activity
    • Z. Oren, J.C. Lerman, G.H. Gudmundsson, B. Agerberth, and Y. Shai Structure and organization of the human antimicrobial peptide LL-37 in phospholipids membranes: relevance to the molecular basis for its non-cell-selective activity Biochem J 341 1999 501 513
    • (1999) Biochem J , vol.341 , pp. 501-513
    • Oren, Z.1    Lerman, J.C.2    Gudmundsson, G.H.3    Agerberth, B.4    Shai, Y.5
  • 18
    • 0032489294 scopus 로고    scopus 로고
    • Mechanism of action of the antimicrobial peptide buforin II: Buforin II kills microorganisms by penetrating the cell membrane and inhibiting cellular functions
    • C.B. Park, H.S. Kim, and S.C. Kim Mechanism of action of the antimicrobial peptide buforin II: buforin II kills microorganisms by penetrating the cell membrane and inhibiting cellular functions Biochem Biophys Res Commun 244 1998 253 257
    • (1998) Biochem Biophys Res Commun , vol.244 , pp. 253-257
    • Park, C.B.1    Kim, H.S.2    Kim, S.C.3
  • 19
    • 0035896642 scopus 로고    scopus 로고
    • Hepcidin, a urinary antimicrobial peptide synthesized in the liver
    • C.H. Park, E.V. Valore, A.J. Waring, and T. Ganz Hepcidin, a urinary antimicrobial peptide synthesized in the liver J Biol Chem 276 2001 7806 7810
    • (2001) J Biol Chem , vol.276 , pp. 7806-7810
    • Park, C.H.1    Valore, E.V.2    Waring, A.J.3    Ganz, T.4
  • 20
    • 1042278915 scopus 로고    scopus 로고
    • The relationship between peptide structure and antibacterial activity
    • J.P.S. Powers, and R.E.W. Hancock The relationship between peptide structure and antibacterial activity Peptides 24 2003 1681 1691
    • (2003) Peptides , vol.24 , pp. 1681-1691
    • Powers, J.P.S.1    Hancock, R.E.W.2
  • 21
    • 0030958619 scopus 로고    scopus 로고
    • Bacterial viability and antibiotic susceptibility testing with SYTOX Green nucleic acid stain
    • B.L. Roth, M. Poot, S.T. Yue, and P.J. Millard Bacterial viability and antibiotic susceptibility testing with SYTOX Green nucleic acid stain Appl Environ Microbiol 63 1997 2421 2431
    • (1997) Appl Environ Microbiol , vol.63 , pp. 2421-2431
    • Roth, B.L.1    Poot, M.2    Yue, S.T.3    Millard, P.J.4
  • 23
    • 27644584146 scopus 로고    scopus 로고
    • Antibacterial activity of human neutrophil defensin HNP-1 analogs without cysteines
    • J. Varkey, and R. Nagaraj Antibacterial activity of human neutrophil defensin HNP-1 analogs without cysteines Antimicrob Agents Chemother 49 2005 4561 4566
    • (2005) Antimicrob Agents Chemother , vol.49 , pp. 4561-4566
    • Varkey, J.1    Nagaraj, R.2
  • 24
    • 39449086721 scopus 로고    scopus 로고
    • Agar and broth dilution methods to determine the minimal inhibitory concentration (MIC) of antimicrobial substances
    • I. Wiegand, K. Hilpert, and R.E. Hancock Agar and broth dilution methods to determine the minimal inhibitory concentration (MIC) of antimicrobial substances Nature Protocols 2 2008 163 174
    • (2008) Nature Protocols , vol.2 , pp. 163-174
    • Wiegand, I.1    Hilpert, K.2    Hancock, R.E.3
  • 25
    • 0042808526 scopus 로고    scopus 로고
    • Engineering disulfide bridges to dissect antimicrobial and chemotactic activities of human beta-defensin 3
    • Z. Wu, D.M. Hoover, D. Yang, C. Boulègue, F. Santamaria, and J.J. Oppenheim Engineering disulfide bridges to dissect antimicrobial and chemotactic activities of human beta-defensin 3 Proc Natl Acad Sci USA 100 2003 8880 8885
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 8880-8885
    • Wu, Z.1    Hoover, D.M.2    Yang, D.3    Boulègue, C.4    Santamaria, F.5    Oppenheim, J.J.6
  • 26
    • 0026550672 scopus 로고
    • Binding of tachyplesin i to DNA revealed by footprinting analysis: Significant contribution of secondary structure to DNA binding and implication for biological action
    • A. Yonezawa, J. Kuwahara, N. Fujii, and Y. Sugiura Binding of tachyplesin I to DNA revealed by footprinting analysis: significant contribution of secondary structure to DNA binding and implication for biological action Biochemistry 31 1992 2998 3004
    • (1992) Biochemistry , vol.31 , pp. 2998-3004
    • Yonezawa, A.1    Kuwahara, J.2    Fujii, N.3    Sugiura, Y.4
  • 27
    • 0023854883 scopus 로고
    • Antimicrobial activity of synthetic magainin peptides and several analogues
    • M. Zasloff, B. Martin, and H.C. Chen Antimicrobial activity of synthetic magainin peptides and several analogues Proc Natl Acad Sci USA 85 1988 910 913
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 910-913
    • Zasloff, M.1    Martin, B.2    Chen, H.C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.