메뉴 건너뛰기




Volumn 69, Issue 6, 2007, Pages 405-412

Hydrophobic interactions in complexes of antimicrobial peptides with bacterial polysaccharides

Author keywords

Alginate; Antimicrobial peptide; Bacterial polysaccharide; Biofilm; Hydrophobic peptide; Peptide saccharide interactions

Indexed keywords

8 ANILINO 1 NAPHTHALENESULFONIC ACID; ALGINIC ACID; BACTERIAL POLYSACCHARIDE; GLYCAN DERIVATIVE; LEUCINE; PHENYLALANINE; POLYPEPTIDE ANTIBIOTIC AGENT; TRYPTOPHAN;

EID: 34250746457     PISSN: 17470277     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1747-0285.2007.00518.x     Document Type: Article
Times cited : (34)

References (45)
  • 1
    • 0029099556 scopus 로고
    • P. aeruginosa mucoidy and the chronic infection phenotype in cystic fibrosis
    • Deretic V., Schurr M.J., Yu H. (1995) P. aeruginosa mucoidy and the chronic infection phenotype in cystic fibrosis. Trends Microbiol 3 : 351 356.
    • (1995) Trends Microbiol , vol.3 , pp. 351-356
    • Deretic, V.1    Schurr, M.J.2    Yu, H.3
  • 2
    • 0034641962 scopus 로고    scopus 로고
    • Quorum-sensing signals indicated that cystic fibrosis lungs are infected with bacterial biofilms
    • Singh P.K., Schaefer A.L., Parsek M.R., Moninger T.O., Welsh M.J., Greenberg E.P. (2000) Quorum-sensing signals indicated that cystic fibrosis lungs are infected with bacterial biofilms. Nature 407 : 762 764.
    • (2000) Nature , vol.407 , pp. 762-764
    • Singh, P.K.1    Schaefer, A.L.2    Parsek, M.R.3    Moninger, T.O.4    Welsh, M.J.5    Greenberg, E.P.6
  • 3
    • 0033591467 scopus 로고    scopus 로고
    • Bacterial biofilms: A common cause of persistent infections
    • Costerton J.W., Stewart P.S., Greenberg E.P. (1999) Bacterial biofilms: a common cause of persistent infections. Science 284 : 1318 1322.
    • (1999) Science , vol.284 , pp. 1318-1322
    • Costerton, J.W.1    Stewart, P.S.2    Greenberg, E.P.3
  • 4
    • 0031801558 scopus 로고    scopus 로고
    • Bacterial alginate biosynthesis-recent progress and future prospects
    • Gacesa P. (1998) Bacterial alginate biosynthesis-recent progress and future prospects. Microbiology 144 : 1133 1143.
    • (1998) Microbiology , vol.144 , pp. 1133-1143
    • Gacesa, P.1
  • 5
    • 0031297640 scopus 로고    scopus 로고
    • Alginate production by Azotobacter vinelandii
    • Clementi F. (1997) Alginate production by Azotobacter vinelandii. Crit Rev Biotechnol 17 : 327 361.
    • (1997) Crit Rev Biotechnol , vol.17 , pp. 327-361
    • Clementi, F.1
  • 6
    • 0019375273 scopus 로고
    • Isolation of alginate-producing mutants of Pseudomonas fluorescens, Pseudomonas putida, and Pseudomonas mendocina
    • Govan J.R., Fyfe J.A., Jarman T.R. (1981) Isolation of alginate-producing mutants of Pseudomonas fluorescens, Pseudomonas putida, and Pseudomonas mendocina. J Gen Microbiol 125 : 217 220.
    • (1981) J Gen Microbiol , vol.125 , pp. 217-220
    • Govan, J.R.1    Fyfe, J.A.2    Jarman, T.R.3
  • 8
    • 0026649046 scopus 로고
    • Pseudomonas aeruginosa biofilm as a diffusion barrier to piperacillin
    • Hoyle B.D., Alcantara H., Costerton J.W. (1992) Pseudomonas aeruginosa biofilm as a diffusion barrier to piperacillin. Antimicrob. Agents Chemother 36 : 2054 2056.
    • (1992) Antimicrob. Agents Chemother , vol.36 , pp. 2054-2056
    • Hoyle, B.D.1    Alcantara, H.2    Costerton, J.W.3
  • 9
    • 0028122702 scopus 로고
    • A Sandwich cup method for the penetration assay of antimicrobial agents through the Pseudomonas exopolysaccharides
    • Kumon H., Tomochika K., Matunaga T., Ogawa M., Ohmori H. (1994) A Sandwich cup method for the penetration assay of antimicrobial agents through the Pseudomonas exopolysaccharides. Microbiol. Immunol. 38 : 615 619.
    • (1994) Microbiol. Immunol. , vol.38 , pp. 615-619
    • Kumon, H.1    Tomochika, K.2    Matunaga, T.3    Ogawa, M.4    Ohmori, H.5
  • 10
    • 0030741702 scopus 로고    scopus 로고
    • Permeation of antimicrobial agents through Pseudomonas aeruginosa biofilms: A simple method
    • Shigeta M., Tanaka G., Komatsuzawa H., Sugai M., Suginaka H., Usui T. (1997) Permeation of antimicrobial agents through Pseudomonas aeruginosa biofilms: a simple method. Chemother 43 : 340 345.
    • (1997) Chemother , vol.43 , pp. 340-345
    • Shigeta, M.1    Tanaka, G.2    Komatsuzawa, H.3    Sugai, M.4    Suginaka, H.5    Usui, T.6
  • 11
    • 0028102175 scopus 로고
    • Investigation of ciprofloxacin penetration into Pseudomonas aeruginosa biofilms
    • Suci P., Mittelman M.W., Yu F.P., Geesy G.G. (1994) Investigation of ciprofloxacin penetration into Pseudomonas aeruginosa biofilms. Antimicrob. Agents Chemother 38 : 2125 2133.
    • (1994) Antimicrob. Agents Chemother , vol.38 , pp. 2125-2133
    • Suci, P.1    Mittelman, M.W.2    Yu, F.P.3    Geesy, G.G.4
  • 12
    • 0031956869 scopus 로고    scopus 로고
    • Alginate lyase promotes diffusion of aminoglycosides through the extracellular polysaccharide of mucoid Pseudomonas aeruginosa
    • Hatch R.A., Schiller N.L. (1998) Alginate lyase promotes diffusion of aminoglycosides through the extracellular polysaccharide of mucoid Pseudomonas aeruginosa. Antimicrob. Agents. Chemother 42 : 974 977.
    • (1998) Antimicrob. Agents. Chemother , vol.42 , pp. 974-977
    • Hatch, R.A.1    Schiller, N.L.2
  • 14
    • 0036840580 scopus 로고    scopus 로고
    • Cationic hydrophobic peptides with antimicrobial activity
    • Stark M., Liu L.P., Deber C.M. (2002) Cationic hydrophobic peptides with antimicrobial activity. Antimicrob Agents Chemother 46 : 3585 90.
    • (2002) Antimicrob Agents Chemother , vol.46 , pp. 3585-90
    • Stark, M.1    Liu, L.P.2    Deber, C.M.3
  • 15
    • 4644245658 scopus 로고    scopus 로고
    • Helix induction in antimicrobial peptides by alginate in biofilms
    • Chan C., Burrows L.L., Deber C.M. (2004) Helix induction in antimicrobial peptides by alginate in biofilms. J Biol Chem 279 : 38749 38754.
    • (2004) J Biol Chem , vol.279 , pp. 38749-38754
    • Chan, C.1    Burrows, L.L.2    Deber, C.M.3
  • 17
    • 0032987478 scopus 로고    scopus 로고
    • Membrane protein folding and stability: Physical principles
    • White S.H., Wimley W.C. (1999) Membrane protein folding and stability: Physical principles. Annu Rev Biophys Biomol Struct 28 : 319 365.
    • (1999) Annu Rev Biophys Biomol Struct , vol.28 , pp. 319-365
    • White, S.H.1    Wimley, W.C.2
  • 18
    • 0025249842 scopus 로고
    • Membrane protein folding and oligomerization: The two-stage model
    • Popot J.L., Engelman D.M. (1990) Membrane protein folding and oligomerization: the two-stage model. Biochemistry 29 : 4031 4037.
    • (1990) Biochemistry , vol.29 , pp. 4031-4037
    • Popot, J.L.1    Engelman, D.M.2
  • 19
    • 16444374940 scopus 로고    scopus 로고
    • Alginate as an auxiliary bacterial membrane: Binding of membrane-active peptides by polysaccharides
    • Chan C., Burrows L.L., Deber C.M. (2005) Alginate as an auxiliary bacterial membrane: binding of membrane-active peptides by polysaccharides. J Pept Res 65 : 343 351.
    • (2005) J Pept Res , vol.65 , pp. 343-351
    • Chan, C.1    Burrows, L.L.2    Deber, C.M.3
  • 20
    • 0030956720 scopus 로고    scopus 로고
    • Anionic phospholipids modulate peptide insertion into membranes
    • Liu L.P., Deber C.M. (1997) Anionic phospholipids modulate peptide insertion into membranes. Biochemistry 36 : 5476 5482.
    • (1997) Biochemistry , vol.36 , pp. 5476-5482
    • Liu, L.P.1    Deber, C.M.2
  • 21
    • 0001376118 scopus 로고
    • Quantitative determination of uronic acid composition of alginate
    • Haug A., Larsen B., Simgsrod O. (1962) Quantitative determination of uronic acid composition of alginate. Acta Chem Scand 16 : 1908 1918.
    • (1962) Acta Chem Scand , vol.16 , pp. 1908-1918
    • Haug, A.1    Larsen, B.2    Simgsrod, O.3
  • 22
    • 0024452212 scopus 로고
    • Adaptation of the Nelson-Somogyi reducing sugar-assay to a microassay using microtiter plates
    • Green F., Clausen C.A., Highley T.L. (1989) Adaptation of the Nelson-Somogyi reducing sugar-assay to a microassay using microtiter plates. Anal Biochem 182 : 197 199.
    • (1989) Anal Biochem , vol.182 , pp. 197-199
    • Green, F.1    Clausen, C.A.2    Highley, T.L.3
  • 23
    • 0037403318 scopus 로고    scopus 로고
    • Determination of the diadic composition of alginate by means of circular dichroism: A fast and accurate improved method
    • Donati I., Gamini A., Skjak-Braek G., Vetere A., Campa C., Coslovi A., Paoletti S. (2003) Determination of the diadic composition of alginate by means of circular dichroism: a fast and accurate improved method. Carbohydr Res 338 : 1139 1142.
    • (2003) Carbohydr Res , vol.338 , pp. 1139-1142
    • Donati, I.1    Gamini, A.2    Skjak-Braek, G.3    Vetere, A.4    Campa, C.5    Coslovi, A.6    Paoletti, S.7
  • 24
    • 0024593221 scopus 로고
    • Purification, characterization, and immunological cross-reactivity of alginates produced by mucoid Pseudomonas aeruginosa from patients with cystic fibrosis
    • Pedersen S.S., Espersen F., Hoiby N., Shaund G.H. (1989) Purification, characterization, and immunological cross-reactivity of alginates produced by mucoid Pseudomonas aeruginosa from patients with cystic fibrosis. J Clin Microb 27 : 691 699.
    • (1989) J Clin Microb , vol.27 , pp. 691-699
    • Pedersen, S.S.1    Espersen, F.2    Hoiby, N.3    Shaund, G.H.4
  • 25
    • 0018394892 scopus 로고
    • A partial modification of the carbazole method of Bitter and Muir for quantification of hexuronic acids
    • Kosakai M., Yoshizawa Z. (1979) A partial modification of the carbazole method of Bitter and Muir for quantification of hexuronic acids. Anal Biochem 93 : 295 298.
    • (1979) Anal Biochem , vol.93 , pp. 295-298
    • Kosakai, M.1    Yoshizawa, Z.2
  • 26
    • 0015794613 scopus 로고
    • Fluorescence and the location of tryptophan residues in protein molecules
    • Burstein E.A., Vedenkina N.S., Ivkova M.N. (1974) Fluorescence and the location of tryptophan residues in protein molecules. Photochem. Photobiol 18 : 263 279.
    • (1974) Photochem. Photobiol , vol.18 , pp. 263-279
    • Burstein, E.A.1    Vedenkina, N.S.2    Ivkova, M.N.3
  • 28
    • 0031568783 scopus 로고    scopus 로고
    • Fluorescence of 8-anilinonaphthalene-1-sulfonate and properties of sodium dodecyl sulfate micelles in water-urea mixtures
    • Abuin E.B., Lissi E.A., Aspee A., Gonzalez F.D., Varas J.M. (1997) Fluorescence of 8-anilinonaphthalene-1-sulfonate and properties of sodium dodecyl sulfate micelles in water-urea mixtures. J Colloid Interface Sci 186 : 332 338.
    • (1997) J Colloid Interface Sci , vol.186 , pp. 332-338
    • Abuin, E.B.1    Lissi, E.A.2    Aspee, A.3    Gonzalez, F.D.4    Varas, J.M.5
  • 29
    • 0016718521 scopus 로고
    • Reversible structural changes in a hydrophobic protein, elastin, as indicated by fluorescence probe analysis
    • Gosline J.M., Yew F.F., Weis-Fogh T. (1975) Reversible structural changes in a hydrophobic protein, elastin, as indicated by fluorescence probe analysis. Biopolymers 14 : 1811 1826.
    • (1975) Biopolymers , vol.14 , pp. 1811-1826
    • Gosline, J.M.1    Yew, F.F.2    Weis-Fogh, T.3
  • 30
    • 0018185273 scopus 로고
    • The use of the fluorescent probe 8-anilinonaphthalene sulfate (ANS) for collagen and elastin histochemistry
    • De Campos Vidal B. (1978) The use of the fluorescent probe 8-anilinonaphthalene sulfate (ANS) for collagen and elastin histochemistry. J Histochem Cytochem 26 : 196 201.
    • (1978) J Histochem Cytochem , vol.26 , pp. 196-201
    • De Campos Vidal, B.1
  • 31
    • 33750819917 scopus 로고    scopus 로고
    • Interaction of native and apo-carbonic anhydrase with hydrophobic adsorbents: A comparative structure-function study
    • Salemi Z, Hosseinkhani S, Ranjbar B, Nemat-Gorgani M. (2006) Interaction of native and apo-carbonic anhydrase with hydrophobic adsorbents: A comparative structure-function study. J Biochem Mol Biol 39 : 636 641.
    • (2006) J Biochem Mol Biol , vol.39 , pp. 636-641
    • Salemi, Z.1    Hosseinkhani, S.2    Ranjbar, B.3    Nemat-Gorgani, M.4
  • 32
    • 0000140515 scopus 로고
    • Hydrophobic folding of maltose in aqueous solution
    • Neal J.L., Goring D.A. (1970) Hydrophobic folding of maltose in aqueous solution. Canadian J Chemistry 48 : 3745 3747.
    • (1970) Canadian J Chemistry , vol.48 , pp. 3745-3747
    • Neal, J.L.1    Goring, D.A.2
  • 34
    • 0007283007 scopus 로고
    • Hydrophobic nature of sugars as evidenced by their differential affinity for polystyrene in aqueous media
    • Masanobu J., Yuki Y. (1985) Hydrophobic nature of sugars as evidenced by their differential affinity for polystyrene in aqueous media. Chem Mat Sci 14 : 891 902.
    • (1985) Chem Mat Sci , vol.14 , pp. 891-902
    • Masanobu, J.1    Yuki, Y.2
  • 36
    • 0026763292 scopus 로고
    • Atomic interactions in protein-carbohydrate complexes. Tryptophan residues in the periplasmic maltodextrin receptor for active transport and chemotaxis
    • Spurlino J.C., Rodseth L.E., Quiocho F.A. (1992) Atomic interactions in protein-carbohydrate complexes. Tryptophan residues in the periplasmic maltodextrin receptor for active transport and chemotaxis. J. Mol. Biol 226 : 15 22.
    • (1992) J. Mol. Biol , vol.226 , pp. 15-22
    • Spurlino, J.C.1    Rodseth, L.E.2    Quiocho, F.A.3
  • 37
    • 0031571605 scopus 로고    scopus 로고
    • Extensive features of tight oligosaccharide binding revealed in high-resolution structures of the maltodextrin transport/chemosensory receptor
    • Quiocho F.A., Spurlino J.C., Rodseth L.E. (1997) Extensive features of tight oligosaccharide binding revealed in high-resolution structures of the maltodextrin transport/chemosensory receptor. Structure 5 : 997 1015.
    • (1997) Structure , vol.5 , pp. 997-1015
    • Quiocho, F.A.1    Spurlino, J.C.2    Rodseth, L.E.3
  • 38
    • 0037458573 scopus 로고    scopus 로고
    • Crystal structure of AlgQ2, a macromolecule (alginate)-binding protein of Sphingomonas sp. A1, complexed with an alginate tetrasaccharide at 1.6 a resolution
    • Mishima Y., Momma K., Hashimoto W., Mikami B., Murata K. (2003) Crystal structure of AlgQ2, a macromolecule (alginate)-binding protein of Sphingomonas sp. A1, complexed with an alginate tetrasaccharide at 1.6 A resolution. J Biol Chem 278 : 6552 6559.
    • (2003) J Biol Chem , vol.278 , pp. 6552-6559
    • Mishima, Y.1    Momma, K.2    Hashimoto, W.3    Mikami, B.4    Murata, K.5
  • 39
    • 0023050603 scopus 로고
    • Monomer sequence and acetylation pattern in some bacterial alginate
    • Skjak-Braek G., Larsen B., Grasdalen H. (1986) Monomer sequence and acetylation pattern in some bacterial alginate. Carbohydr Res 154 : 239 250.
    • (1986) Carbohydr Res , vol.154 , pp. 239-250
    • Skjak-Braek, G.1    Larsen, B.2    Grasdalen, H.3
  • 40
    • 0031926765 scopus 로고    scopus 로고
    • Guidelines for membrane protein engineering derived from de novo designed model peptides
    • Liu L.P., Deber C.M. (1998) Guidelines for membrane protein engineering derived from de novo designed model peptides. Biopolymers 47 : 41 62.
    • (1998) Biopolymers , vol.47 , pp. 41-62
    • Liu, L.P.1    Deber, C.M.2
  • 41
    • 0035683866 scopus 로고    scopus 로고
    • Hydrogels for biomedical applications
    • Hoffman A.S. (2001) Hydrogels for biomedical applications. Ann N.Y. Acad Sci 944 : 62 73.
    • (2001) Ann N.Y. Acad Sci , vol.944 , pp. 62-73
    • Hoffman, A.S.1
  • 42
    • 33746474818 scopus 로고    scopus 로고
    • Polyanionic hydrocolloids for the intestinal delivery of protein drugs: Alginate-chitosan - A review
    • Meera G., Abraham T.E. (2006) Polyanionic hydrocolloids for the intestinal delivery of protein drugs: alginate-chitosan - a review. J Control Release 114 : 1 14.
    • (2006) J Control Release , vol.114 , pp. 1-14
    • Meera, G.1    Abraham, T.E.2
  • 43
    • 0030070010 scopus 로고    scopus 로고
    • Characterization of the sources of protein-ligand affinity: 1-sulfonato-8-anilinonapthalene binding to intestinal fatty acid binding protein
    • Kirk W.R., Kurian E., Prendergast F.G. (1996) Characterization of the sources of protein-ligand affinity: 1-sulfonato-8-anilinonapthalene binding to intestinal fatty acid binding protein. Biophys J 70 : 69 83.
    • (1996) Biophys J , vol.70 , pp. 69-83
    • Kirk, W.R.1    Kurian, E.2    Prendergast, F.G.3
  • 44
    • 0031972919 scopus 로고    scopus 로고
    • 1-Anilino-8-napthalene sulfonate anion-protein binding depends primarily on ion pair formation
    • Matulis D., Lovrien R. (1998) 1-Anilino-8-napthalene sulfonate anion-protein binding depends primarily on ion pair formation. Biophys J 74 : 422 429.
    • (1998) Biophys J , vol.74 , pp. 422-429
    • Matulis, D.1    Lovrien, R.2
  • 45
    • 0037403860 scopus 로고    scopus 로고
    • A fluorescence study of the interactions between sodium alginate and surfactants
    • Neumann M.G., Schmitt C.C., Iamazaki E.T. (2003) A fluorescence study of the interactions between sodium alginate and surfactants. Carbohydr Res 338 : 1109 1113.
    • (2003) Carbohydr Res , vol.338 , pp. 1109-1113
    • Neumann, M.G.1    Schmitt, C.C.2    Iamazaki, E.T.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.