메뉴 건너뛰기




Volumn 19, Issue 12, 2013, Pages 792-800

Inhibitory effect of short cationic homopeptides against Gram-positive bacteria

Author keywords

antibacterial peptides; Arg; cationic homopeptides; Gram positive bacteria; Lys; polyproline II helix

Indexed keywords

AMINO ACID; ARGININE; LIPOSOME; LYSINE; POLYPEPTIDE ANTIBIOTIC AGENT; PROLINE;

EID: 84888050522     PISSN: 10752617     EISSN: 10991387     Source Type: Journal    
DOI: 10.1002/psc.2578     Document Type: Article
Times cited : (27)

References (39)
  • 1
    • 70349637842 scopus 로고    scopus 로고
    • De novo generation of antimicrobial LK peptides with a single tryptophan at the critical amphipatic interface
    • Kang SJ, Won HS, Choi WS, Lee BJ,. De novo generation of antimicrobial LK peptides with a single tryptophan at the critical amphipatic interface. J. Pept. Sci. 2009; 15: 583-588.
    • (2009) J. Pept. Sci. , vol.15 , pp. 583-588
    • Kang, S.J.1    Won, H.S.2    Choi, W.S.3    Lee, B.J.4
  • 2
    • 78650179473 scopus 로고    scopus 로고
    • De novo generation of short antimicrobial peptides with simple amino acid composition
    • Lee SH, Kim SJ, Lee s, Song M, Kim IH, Won HS,. De novo generation of short antimicrobial peptides with simple amino acid composition. Regul. Pept. 2011; 166: 36-41.
    • (2011) Regul. Pept. , vol.166 , pp. 36-41
    • Lee, S.H.1    Kim, S.J.2    Lee, S.3    Song, M.4    Kim, I.H.5    Won, H.S.6
  • 4
    • 79960934532 scopus 로고    scopus 로고
    • Short native antimicrobial peptides and engineered ultrashort lipopeptides: Similarities and differences in cell specificities and modes of action
    • Mangoni M, Shai Y,. Short native antimicrobial peptides and engineered ultrashort lipopeptides: similarities and differences in cell specificities and modes of action. Cell. Mol. Life Sci. 2011; 68: 2267-2280.
    • (2011) Cell. Mol. Life Sci. , vol.68 , pp. 2267-2280
    • Mangoni, M.1    Shai, Y.2
  • 5
    • 69349092183 scopus 로고    scopus 로고
    • Coupling molecular dynamic simulations with experiments for the rational design of indolicidin-analogous antimicrobial peptides
    • Tsai CW, Hsu NY, Wang CH, Lu CY, Chang Y, Tsai HHG, Ruaan RC,. Coupling molecular dynamic simulations with experiments for the rational design of indolicidin-analogous antimicrobial peptides. J. Mol. Biol. 2009; 392: 837-54.
    • (2009) J. Mol. Biol. , vol.392 , pp. 837-854
    • Tsai, C.W.1    Hsu, N.Y.2    Wang, C.H.3    Lu, C.Y.4    Chang, Y.5    Tsai, H.H.G.6    Ruaan, R.C.7
  • 6
    • 78650101939 scopus 로고    scopus 로고
    • Protein homorepeats: Sequences, structures, evolution, and functions
    • Jorda J, Kajava AV, Protein homorepeats: sequences, structures, evolution, and functions. Adv. Protein Chem. Struct. Biol. 2010; 79: 59-88.
    • (2010) Adv. Protein Chem. Struct. Biol. , vol.79 , pp. 59-88
    • Jorda, J.1    Kajava, A.V.2
  • 7
    • 76549252207 scopus 로고
    • The structure of proteins: Two hydrogen bonded helical configurations of the polypeptide chain
    • Pauling L, Corey RB, Branson HR,. The structure of proteins: two hydrogen bonded helical configurations of the polypeptide chain. Natl. Acad. Sci. USA 1951; 37: 2005-2011.
    • (1951) Natl. Acad. Sci. USA , vol.37 , pp. 2005-2011
    • Pauling, L.1    Corey, R.B.2    Branson, H.R.3
  • 8
    • 0032693639 scopus 로고    scopus 로고
    • Why and how are peptide-lipid interactions utilized for self-defense? Magainins and tachyplesins as archetypes
    • Matsuzaki K,. Why and how are peptide-lipid interactions utilized for self-defense? Magainins and tachyplesins as archetypes. Biochim. Biophys. Acta 1999; 1462: 1-10.
    • (1999) Biochim. Biophys. Acta , vol.1462 , pp. 1-10
    • Matsuzaki, K.1
  • 9
    • 46349095009 scopus 로고    scopus 로고
    • Membrane interaction and perturbation mechanisms induced by two cationic cell penetrating peptides with distinct charge distribution
    • Alves ID, Goasdoue N, Correia I, Aubry S, Galanth C, Sagan S, Lavielle S, Chassaing G,. Membrane interaction and perturbation mechanisms induced by two cationic cell penetrating peptides with distinct charge distribution. Biochim. Biophys. Acta 2008; 1780: 948-959.
    • (2008) Biochim. Biophys. Acta , vol.1780 , pp. 948-959
    • Alves, I.D.1    Goasdoue, N.2    Correia, I.3    Aubry, S.4    Galanth, C.5    Sagan, S.6    Lavielle, S.7    Chassaing, G.8
  • 10
    • 84869861771 scopus 로고    scopus 로고
    • Antimicrobial and cell-penetrating properties of penetratin analogs: Effect of sequence and secondary structure
    • Bahnsen JS, Franzyk H, Sandberg-Schaal A, Nielsen HM,. Antimicrobial and cell-penetrating properties of penetratin analogs: effect of sequence and secondary structure. Biochim. Biophys. Acta 2013; 1828: 223-232.
    • (2013) Biochim. Biophys. Acta , vol.1828 , pp. 223-232
    • Bahnsen, J.S.1    Franzyk, H.2    Sandberg-Schaal, A.3    Nielsen, H.M.4
  • 11
    • 38949116621 scopus 로고    scopus 로고
    • Thermodynamic studies and binding mechanisms of cell-penetrating peptides with lipids and glycosaminoglycans
    • Ziegler A,. Thermodynamic studies and binding mechanisms of cell-penetrating peptides with lipids and glycosaminoglycans. Adv. Drug Deliv. Rev. 2008; 60: 580-97.
    • (2008) Adv. Drug Deliv. Rev. , vol.60 , pp. 580-597
    • Ziegler, A.1
  • 12
    • 67650361680 scopus 로고    scopus 로고
    • A novel antifungal peptide designed from the primary structure of a natural antimicrobial peptide purified from Argopecten purpuratus hemocytes
    • Arenas G, Guzmán F, Cárdenas C, Mercado L, Marshall SH,. A novel antifungal peptide designed from the primary structure of a natural antimicrobial peptide purified from Argopecten purpuratus hemocytes. Peptides 2009; 30: 1405-1411.
    • (2009) Peptides , vol.30 , pp. 1405-1411
    • Arenas, G.1    Guzmán, F.2    Cárdenas, C.3    Mercado, L.4    Marshall, S.H.5
  • 13
    • 0032522765 scopus 로고    scopus 로고
    • Bactericidal activity of Lys49 and Asp49 myotoxic phospholipases A(2) from Bothrops asper snake venom - Synthetic Lys49 myotoxin II-(115-129)-peptide identifies its bactericidal region
    • Páramo L, Lomonte B, Pizarro-Cerdá J, Bengoechea JA, Gorvel JP, Moreno E,. Bactericidal activity of Lys49 and Asp49 myotoxic phospholipases A(2) from Bothrops asper snake venom-synthetic Lys49 myotoxin II-(115-129)-peptide identifies its bactericidal region. Eur. J. Biochem. 1998; 253: 452-61.
    • (1998) Eur. J. Biochem. , vol.253 , pp. 452-461
    • Páramo, L.1    Lomonte, B.2    Pizarro-Cerdá, J.3    Bengoechea, J.A.4    Gorvel, J.P.5    Moreno, E.6
  • 15
    • 0036404956 scopus 로고    scopus 로고
    • Characterization of Vibrio mimicus phospholipase A (PhlA) and cytotoxicity on fish cell
    • Lee J, Ahn S, Kim S, Choi Y, Park K, Kong I,. Characterization of Vibrio mimicus phospholipase A (PhlA) and cytotoxicity on fish cell. Biochem. Biophys. Res. Commun. 2002; 298: 269-276.
    • (2002) Biochem. Biophys. Res. Commun. , vol.298 , pp. 269-276
    • Lee, J.1    Ahn, S.2    Kim, S.3    Choi, Y.4    Park, K.5    Kong, I.6
  • 16
    • 0022452397 scopus 로고
    • Prediction of peptide retention times in reversed-phase high-performance liquid chromatography I. Determination of retention coefficients of amino acid residues of model synthetic peptides
    • Guo D, Mant C, Taneja A, Parker J, Rodges R,. Prediction of peptide retention times in reversed-phase high-performance liquid chromatography I. Determination of retention coefficients of amino acid residues of model synthetic peptides. J. Chromatogr. A 1986; 359: 499-518.
    • (1986) J. Chromatogr. A , vol.359 , pp. 499-518
    • Guo, D.1    Mant, C.2    Taneja, A.3    Parker, J.4    Rodges, R.5
  • 17
    • 0023055775 scopus 로고
    • New hydrophilicity scale derived from high-performance liquid chromatography peptide retention data: Correlation of predicted surface residues with antigenicity and X-ray-derived accessible sites
    • Parker JM, Guo D, Hodges RS,. New hydrophilicity scale derived from high-performance liquid chromatography peptide retention data: correlation of predicted surface residues with antigenicity and X-ray-derived accessible sites. Biochemistry 1986; 25: 5425-5432.
    • (1986) Biochemistry , vol.25 , pp. 5425-5432
    • Parker, J.M.1    Guo, D.2    Hodges, R.S.3
  • 18
    • 0016276163 scopus 로고
    • The calculated circular dichroism of polyproline II in the polarizability approximation
    • Ronish EW, Krimm S,. The calculated circular dichroism of polyproline II in the polarizability approximation. Biopolymers 1974; 13: 1635-1651.
    • (1974) Biopolymers , vol.13 , pp. 1635-1651
    • Ronish, E.W.1    Krimm, S.2
  • 19
    • 0036129072 scopus 로고    scopus 로고
    • Polyproline II helical structure in protein unfolded states: Lysine peptides revisited
    • Rucker AL, Creamer TP,. Polyproline II helical structure in protein unfolded states: lysine peptides revisited. Protein Sci. 2002; 11: 980-985.
    • (2002) Protein Sci. , vol.11 , pp. 980-985
    • Rucker, A.L.1    Creamer, T.P.2
  • 22
    • 0346688716 scopus 로고    scopus 로고
    • Interaction of the protein transduction domain of HIV-1 TAT with heparin sulfate: Binding mechanism and thermodynamic parameters
    • Ziegler A, Seelig J,. Interaction of the protein transduction domain of HIV-1 TAT with heparin sulfate: binding mechanism and thermodynamic parameters. Biophys. J. 2004; 86: 254-63.
    • (2004) Biophys. J. , vol.86 , pp. 254-263
    • Ziegler, A.1    Seelig, J.2
  • 23
    • 37349034233 scopus 로고    scopus 로고
    • Cell envelope stress response in Gram-positive bacteria
    • Jordan S, Hutchings MI, Mascher T,. Cell envelope stress response in Gram-positive bacteria. FEMS Microbiol. Rev. 2008; 32: 107-146.
    • (2008) FEMS Microbiol. Rev. , vol.32 , pp. 107-146
    • Jordan, S.1    Hutchings, M.I.2    Mascher, T.3
  • 24
    • 65249175757 scopus 로고    scopus 로고
    • Cell specificity, anti-inflammatory activity, and plausible bactericidal mechanism of designed Trp-rich model antimicrobial peptides
    • Park KH, Nan YH, Park Y, Kim JI, Park IS, Hahm KS, Shin SY,. Cell specificity, anti-inflammatory activity, and plausible bactericidal mechanism of designed Trp-rich model antimicrobial peptides. Biochim. Biophys. Acta 2009; 1788: 1193-1203.
    • (2009) Biochim. Biophys. Acta , vol.1788 , pp. 1193-1203
    • Park, K.H.1    Nan, Y.H.2    Park, Y.3    Kim, J.I.4    Park, I.S.5    Hahm, K.S.6    Shin, S.Y.7
  • 25
    • 33746698355 scopus 로고    scopus 로고
    • A polarized-light spectroscopy study of interactions of a hairpin polyamide with DNA
    • Caesar C, Johnsson R, Ellervik U, Fox K, Lincoln P, Nordén B,. A polarized-light spectroscopy study of interactions of a hairpin polyamide with DNA. Biophys. J. 2006; 91: 904-911.
    • (2006) Biophys. J. , vol.91 , pp. 904-911
    • Caesar, C.1    Johnsson, R.2    Ellervik, U.3    Fox, K.4    Lincoln, P.5    Nordén, B.6
  • 26
    • 0033864862 scopus 로고    scopus 로고
    • Amphipathic, alpha-helical antimicrobial peptides
    • Tossi A, Sandri L, Giangaspero A,. Amphipathic, alpha-helical antimicrobial peptides. Biopolymers 2000; 55: 4-30.
    • (2000) Biopolymers , vol.55 , pp. 4-30
    • Tossi, A.1    Sandri, L.2    Giangaspero, A.3
  • 28
    • 70350040736 scopus 로고    scopus 로고
    • Cell penetrating peptides: How do they do it?
    • Herce HD, Garcia AE,. Cell penetrating peptides: how do they do it? J. Biol. Phys. 2007; 33: 345-356.
    • (2007) J. Biol. Phys. , vol.33 , pp. 345-356
    • Herce, H.D.1    Garcia, A.E.2
  • 29
    • 82155176225 scopus 로고    scopus 로고
    • Comparative study on the interaction of cell-penetrating polycationic polymers with lipid membranes
    • Takechi, Y,;, Tanaka, H, Kitayama, Hiroki K, Haruka Y, Masafumi T, Hiroyuki S,. Comparative study on the interaction of cell-penetrating polycationic polymers with lipid membranes. Chem. Phys. Lipids 2012; 165: 51-55.
    • (2012) Chem. Phys. Lipids , vol.165 , pp. 51-55
    • Takechi, Y.1    Tanaka, H.2    Kitayama3    Hiroki, K.4    Haruka, Y.5    Masafumi, T.6    Hiroyuki, S.7
  • 30
    • 84872237583 scopus 로고    scopus 로고
    • Structure-activity relationships of the antimicrobial peptide arasin 1 - And mode of action studies of the N-terminal, proline-rich region
    • Paulsen VS, Blencke HM, Benincasa M, Haug T, Eksteen JJ, Styrvold OB, Scocchi M, Stensvag K,. Structure-activity relationships of the antimicrobial peptide arasin 1-and mode of action studies of the N-terminal, proline-rich region. Plos One. 2013; 8: 1-11.
    • (2013) Plos One. , vol.8 , pp. 1-11
    • Paulsen, V.S.1    Blencke, H.M.2    Benincasa, M.3    Haug, T.4    Eksteen, J.J.5    Styrvold, O.B.6    Scocchi, M.7    Stensvag, K.8
  • 31
    • 37349104237 scopus 로고    scopus 로고
    • Alternative mechanisms of action of cationic antimicrobial peptides on bacteria
    • Hale JD, Hancock RE,. Alternative mechanisms of action of cationic antimicrobial peptides on bacteria. Expert Rev. Anti Infect. Ther. 2007; 5: 951-959.
    • (2007) Expert Rev. Anti Infect. Ther. , vol.5 , pp. 951-959
    • Hale, J.D.1    Hancock, R.E.2
  • 32
    • 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
    • Park CB, Kim HS, Kim SC,. 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. 1998; 244: 253-257.
    • (1998) Biochem. Biophys. Res. Commun. , vol.244 , pp. 253-257
    • Park, C.B.1    Kim, H.S.2    Kim, S.C.3
  • 33
    • 3343017389 scopus 로고    scopus 로고
    • Consequences of nonlytic membrane perturbation to the translocation of the cell penetrating peptide pep-1 in lipidic vesicles
    • Henriques ST, Castanho MA,. Consequences of nonlytic membrane perturbation to the translocation of the cell penetrating peptide pep-1 in lipidic vesicles. Biochemistry 2004; 43: 9716-9724.
    • (2004) Biochemistry , vol.43 , pp. 9716-9724
    • Henriques, S.T.1    Castanho, M.A.2
  • 34
    • 67849090376 scopus 로고    scopus 로고
    • Poly- l -lysines and poly- l -arginines induce leakage of negatively charged phospholipid vesicles and translocate through the lipid bilayer upon electrostatic binding to the membrane
    • Reuter M, Schwieger C, Meister A, Karlsson G, Blume A,. Poly- l -lysines and poly- l -arginines induce leakage of negatively charged phospholipid vesicles and translocate through the lipid bilayer upon electrostatic binding to the membrane. Biophys. Chem. 2009; 144: 27-37.
    • (2009) Biophys. Chem. , vol.144 , pp. 27-37
    • Reuter, M.1    Schwieger, C.2    Meister, A.3    Karlsson, G.4    Blume, A.5
  • 35
    • 77952955984 scopus 로고    scopus 로고
    • Identification of residues critical for the cell-membrane-penetrating activity of zebrafish neuroglobin
    • Watanabe S, Wakasugi K,. Identification of residues critical for the cell-membrane-penetrating activity of zebrafish neuroglobin. FEBS Lett. 2010; 584: 2467-2472.
    • (2010) FEBS Lett. , vol.584 , pp. 2467-2472
    • Watanabe, S.1    Wakasugi, K.2
  • 38
    • 66349138469 scopus 로고    scopus 로고
    • Roles of arginine and lysine residues in the translocation of a cell-penetrating peptide from (13)C, (31)P, and (19)F solid-state NMR
    • Su Y, Doherty T, Waring AJ, Ruchala P, Hong M,. Roles of arginine and lysine residues in the translocation of a cell-penetrating peptide from (13)C, (31)P, and (19)F solid-state NMR. Biochemistry 2009; 48: 4587-4595.
    • (2009) Biochemistry , vol.48 , pp. 4587-4595
    • Su, Y.1    Doherty, T.2    Waring, A.J.3    Ruchala, P.4    Hong, M.5
  • 39
    • 84877253467 scopus 로고    scopus 로고
    • Polyarginine molecular weight determines transfection efficiency of calcium condensed complexes
    • Alhakamy NA, Berkland CJ,. Polyarginine molecular weight determines transfection efficiency of calcium condensed complexes. Mol. Pharmaceutic. 2013; 10: 1940-1948.
    • (2013) Mol. Pharmaceutic. , vol.10 , pp. 1940-1948
    • Alhakamy, N.A.1    Berkland, C.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.