메뉴 건너뛰기




Volumn 89, Issue 6, 2013, Pages 1433-1441

Impact of dye-protein interaction and silver nanoparticles on rose bengal photophysical behavior and protein photocrosslinking

Author keywords

[No Author keywords available]

Indexed keywords

STAPHYLOCOCCUS EPIDERMIDIS;

EID: 84887407189     PISSN: 00318655     EISSN: 17511097     Source Type: Journal    
DOI: 10.1111/php.12119     Document Type: Article
Times cited : (21)

References (46)
  • 3
    • 79960284892 scopus 로고    scopus 로고
    • Effect of temperature on the photobehavior of rose bengal associated with dipalmitoylphosphatidyl choline liposomes
    • Hugo, E., E. Abuin, E. Lissi, E. Alarcon, and, A. M. Edwards, (2011) Effect of temperature on the photobehavior of rose bengal associated with dipalmitoylphosphatidyl choline liposomes. J. Lumin. 131, 2468-2472.
    • (2011) J. Lumin. , vol.131 , pp. 2468-2472
    • Hugo, E.1    Abuin, E.2    Lissi, E.3    Alarcon, E.4    Edwards, A.M.5
  • 4
    • 0030971223 scopus 로고    scopus 로고
    • Excited triplet state photophysics of the sulphonated aluminium phthalocyanines bound to human serum albumin
    • Foley, M. S. C., A. Beeby, A. W. Parker, S. M. Bishop, and, D. Phillips, (1997) Excited triplet state photophysics of the sulphonated aluminium phthalocyanines bound to human serum albumin. J. Photoch. Photobiol. B. 38, 10-17.
    • (1997) J. Photoch. Photobiol. B. , vol.38 , pp. 10-17
    • Foley, M.S.C.1    Beeby, A.2    Parker, A.W.3    Bishop, S.M.4    Phillips, D.5
  • 7
    • 0025104818 scopus 로고
    • Photoreactions of macrocyclic dyes bound to human serum albumin
    • Davila, J., and, A. Harriman, (1990) Photoreactions of macrocyclic dyes bound to human serum albumin. Photochem. Photobiol. 51, 9-19.
    • (1990) Photochem. Photobiol. , vol.51 , pp. 9-19
    • Davila, J.1    Harriman, A.2
  • 8
    • 84869987790 scopus 로고    scopus 로고
    • Photoinduced protein modifications by methylene blue and naproxen
    • Bracchitta, G., A. Catalfo, and, G. De Guidi, (2012) Photoinduced protein modifications by methylene blue and naproxen. Photoch. Photobio. Sci. 11, 1886-1896.
    • (2012) Photoch. Photobio. Sci. , vol.11 , pp. 1886-1896
    • Bracchitta, G.1    Catalfo, A.2    De Guidi, G.3
  • 9
    • 84871546396 scopus 로고    scopus 로고
    • Human serum albumin as protecting agent of silver nanoparticles: Role of the protein conformation and amine groups in the nanoparticle stabilization
    • Alarcon, E., C. Bueno-Alejo, C. Noel, K. Stamplecoskie, N. Pacioni, H. Poblete, and, J. C. Scaiano, (2013) Human serum albumin as protecting agent of silver nanoparticles: Role of the protein conformation and amine groups in the nanoparticle stabilization. J. Nanopart. Res. 15, 1-14.
    • (2013) J. Nanopart. Res. , vol.15 , pp. 1-14
    • Alarcon, E.1    Bueno-Alejo, C.2    Noel, C.3    Stamplecoskie, K.4    Pacioni, N.5    Poblete, H.6    Scaiano, J.C.7
  • 12
    • 0030199820 scopus 로고    scopus 로고
    • Photodynamic crosslinking of proteins. I. Model studies using histidine- and lysine-containing n-(2-hydroxypropyl) methacrylamide copolymers
    • Shen, H.-R., J. D. Spikes, P. Kopecekova, and, J. Kopecek, (1996) Photodynamic crosslinking of proteins. I. Model studies using histidine- and lysine-containing n-(2-hydroxypropyl) methacrylamide copolymers. J. Photochem. Photobiol., B 34, 203-210.
    • (1996) J. Photochem. Photobiol., B , vol.34 , pp. 203-210
    • Shen, H.-R.1    Spikes, J.D.2    Kopecekova, P.3    Kopecek, J.4
  • 13
    • 0003078737 scopus 로고    scopus 로고
    • Photodynamic crosslinking of proteins ii. Photocrosslinking of a model protein-ribonuclease a
    • Shen, H.-R., J. D. Spikes, P. Kopecekova, and, J. Kopecek, (1996) Photodynamic crosslinking of proteins ii. Photocrosslinking of a model protein-ribonuclease a. J. Photochem. Photobiol., B 35, 213-219.
    • (1996) J. Photochem. Photobiol., B , vol.35 , pp. 213-219
    • Shen, H.-R.1    Spikes, J.D.2    Kopecekova, P.3    Kopecek, J.4
  • 14
    • 0033173599 scopus 로고    scopus 로고
    • Photodynamic crosslinking of proteins. Iii. Kinetics of the fmn- and rose bengal-sensitized photooxidation and intermolecular crosslinking of model tyrosine-containing n-(2-hydroxypropyl)methacrylamide copolymers
    • Spikes, J. D., H.-R. Shen, P. Kopecekova, and, J. Kopecek, (1999) Photodynamic crosslinking of proteins. Iii. Kinetics of the fmn- and rose bengal-sensitized photooxidation and intermolecular crosslinking of model tyrosine-containing n-(2-hydroxypropyl)methacrylamide copolymers. Photochem. Photobiol. 70, 130-137.
    • (1999) Photochem. Photobiol. , vol.70 , pp. 130-137
    • Spikes, J.D.1    Shen, H.-R.2    Kopecekova, P.3    Kopecek, J.4
  • 15
    • 77952032620 scopus 로고    scopus 로고
    • Collagen cross-linking: A new treatment paradigm in corneal disease - A review
    • Snibson, G. R., (2010) Collagen cross-linking: A new treatment paradigm in corneal disease-a review. Clin. Exp. Ophthal. 38, 141-153.
    • (2010) Clin. Exp. Ophthal. , vol.38 , pp. 141-153
    • Snibson, G.R.1
  • 16
    • 84985451848 scopus 로고
    • Model studies on photodynamic cross-linking
    • Verweu, H., and, J. v. Steveninck, (1982) Model studies on photodynamic cross-linking. Photochem. Photobiol. 35, 265-267.
    • (1982) Photochem. Photobiol. , vol.35 , pp. 265-267
    • Verweu, H.1    Steveninck, J.V.2
  • 18
    • 34548087293 scopus 로고    scopus 로고
    • Photochemically cross-linked collagen gels as three-dimensional scaffolds for tissue engineering
    • Ibusuki, S., G. J. Halbesma, M. A. Randolph, R. W. Redmond, I. E. Kochevar, and, T. J. Gill, (2007) Photochemically cross-linked collagen gels as three-dimensional scaffolds for tissue engineering. Tissue Eng. 13, 1995-2001.
    • (2007) Tissue Eng. , vol.13 , pp. 1995-2001
    • Ibusuki, S.1    Halbesma, G.J.2    Randolph, M.A.3    Redmond, R.W.4    Kochevar, I.E.5    Gill, T.J.6
  • 20
  • 21
    • 79959320261 scopus 로고    scopus 로고
    • Photochemical tissue bonding: A potential strategy for treating limbal stem cell deficiency
    • Gu, C., T. Ni, E. E. Verter, R. W. Redmond, I. E. Kochevar, and, M. Yao, (2011) Photochemical tissue bonding: A potential strategy for treating limbal stem cell deficiency. Lasers Surg. Med. 43, 433-442.
    • (2011) Lasers Surg. Med. , vol.43 , pp. 433-442
    • Gu, C.1    Ni, T.2    Verter, E.E.3    Redmond, R.W.4    Kochevar, I.E.5    Yao, M.6
  • 22
    • 79960501483 scopus 로고    scopus 로고
    • A light-activated method for repair of corneal surface defects
    • Wang, Y., I. E. Kochevar, R. W. Redmond, and, M. Yao, (2011) A light-activated method for repair of corneal surface defects. Lasers Surg. Med. 43, 481-489.
    • (2011) Lasers Surg. Med. , vol.43 , pp. 481-489
    • Wang, Y.1    Kochevar, I.E.2    Redmond, R.W.3    Yao, M.4
  • 24
    • 0001372680 scopus 로고
    • Aggregation of rose bengal molecules in solution
    • Xu, D., and, D. C. Neckers, (1987) Aggregation of rose bengal molecules in solution. J. Photochem. Photobiol., A 40, 361-370.
    • (1987) J. Photochem. Photobiol., A , vol.40 , pp. 361-370
    • Xu, D.1    Neckers, D.C.2
  • 25
    • 84986522918 scopus 로고
    • Icm - A new method for protein modeling and design: Applications to docking and structure prediction from the distorted native conformation
    • Abagyan, R., M. Totrov, and, D. Kuznetsov, (1994) Icm-a new method for protein modeling and design: Applications to docking and structure prediction from the distorted native conformation. J. Comp. Chem. 15, 488-506.
    • (1994) J. Comp. Chem. , vol.15 , pp. 488-506
    • Abagyan, R.1    Totrov, M.2    Kuznetsov, D.3
  • 26
    • 0027996196 scopus 로고
    • Crystal and molecular structure of a collagen-like peptide at 1.9 a resolution
    • Bella, J., M. Eaton, B. Brodsky, and, H. M. Berman, (1994) Crystal and molecular structure of a collagen-like peptide at 1.9 a resolution. Science 266, 75-81.
    • (1994) Science , vol.266 , pp. 75-81
    • Bella, J.1    Eaton, M.2    Brodsky, B.3    Berman, H.M.4
  • 27
    • 0001731773 scopus 로고
    • Energy parameters in polypeptides. 10. Improved geometrical parameters and nonbonded interactions for use in the ecepp/3 algorithm, with application to proline-containing peptides
    • Nemethy, G., K. D. Gibson, K. A. Palmer, C. N. Yoon, G. Paterlini, A. Zagari, S. Rumsey, and, H. A. Scheraga, (1992) Energy parameters in polypeptides. 10. Improved geometrical parameters and nonbonded interactions for use in the ecepp/3 algorithm, with application to proline-containing peptides. J. Phys. Chem. 96, 6472-6484.
    • (1992) J. Phys. Chem. , vol.96 , pp. 6472-6484
    • Nemethy, G.1    Gibson, K.D.2    Palmer, K.A.3    Yoon, C.N.4    Paterlini, G.5    Zagari, A.6    Rumsey, S.7    Scheraga, H.A.8
  • 28
    • 0027955787 scopus 로고
    • Biased probability monte carlo conformational searches and electrostatic calculations for peptides and proteins
    • Abagyan, R., and, M. Totrov, (1994) Biased probability monte carlo conformational searches and electrostatic calculations for peptides and proteins. J. Mol. Biol. 235, 983-1002.
    • (1994) J. Mol. Biol. , vol.235 , pp. 983-1002
    • Abagyan, R.1    Totrov, M.2
  • 29
    • 84155167320 scopus 로고    scopus 로고
    • Evaluation of solute binding to proteins and intra-protein distances from steady state fluoresence measurements
    • Alarcon, E., A. Aspee, E. A. Abuin, and, E. A. Lissi, (2012) Evaluation of solute binding to proteins and intra-protein distances from steady state fluoresence measurements. J. Photoch. Photobiol. B. 106, 1-7.
    • (2012) J. Photoch. Photobiol. B. , vol.106 , pp. 1-7
    • Alarcon, E.1    Aspee, A.2    Abuin, E.A.3    Lissi, E.A.4
  • 30
    • 0026632930 scopus 로고
    • Ferrous oxidation in the presence of xylenol orange for detection of lipid hydroperoxides in low density lipoproteins
    • Jiang, Y., J. V. Hunt, and, S. P. Wolff, (1992) Ferrous oxidation in the presence of xylenol orange for detection of lipid hydroperoxides in low density lipoproteins. Anal. Biochem. 202, 384-389.
    • (1992) Anal. Biochem. , vol.202 , pp. 384-389
    • Jiang, Y.1    Hunt, J.V.2    Wolff, S.P.3
  • 31
    • 29244444522 scopus 로고    scopus 로고
    • Fluorescence probes used for detection of reactive oxygen species
    • Gomes, A., E. Fernandes, and, J. L. F. C. Lima, (2005) Fluorescence probes used for detection of reactive oxygen species. J. Biochem. Biophys. Methods 65, 45-80.
    • (2005) J. Biochem. Biophys. Methods , vol.65 , pp. 45-80
    • Gomes, A.1    Fernandes, E.2    Lima, J.L.F.C.3
  • 32
    • 0041935939 scopus 로고    scopus 로고
    • U.S. National Institutes of Health, Bethesda, MA
    • Rasband, W. S., (1997-2009) Imagej, U.S. National Institutes of Health, Bethesda, MA.
    • (1997) Imagej
    • Rasband, W.S.1
  • 35
    • 0027002715 scopus 로고
    • Crosslinking of collagen gels: Photochemical measurements
    • Milne, P. J., and, R. G. Zika, (1992) Crosslinking of collagen gels: Photochemical measurements. Proc. SPIE 1644, 115-124.
    • (1992) Proc. SPIE , vol.1644 , pp. 115-124
    • Milne, P.J.1    Zika, R.G.2
  • 38
    • 33947093673 scopus 로고
    • Hydrogen bond strengths from solvent dependence lifetimes of rose bengal dye
    • Cramer, L. E., and, K. G. Spears, (1978) Hydrogen bond strengths from solvent dependence lifetimes of rose bengal dye. J. Am. Chem. Soc. 100, 221-222.
    • (1978) J. Am. Chem. Soc. , vol.100 , pp. 221-222
    • Cramer, L.E.1    Spears, K.G.2
  • 39
    • 0002668561 scopus 로고    scopus 로고
    • Solvent effects on rates of photochemical reactions of rose bengal triplet state studied by nanosecond laser photolysis
    • Islam, S. D.-M., and, O. Ito, (1999) Solvent effects on rates of photochemical reactions of rose bengal triplet state studied by nanosecond laser photolysis. J. Photochem. Photobiol., A 123, 53-59.
    • (1999) J. Photochem. Photobiol., A , vol.123 , pp. 53-59
    • Islam, S.D.-M.1    Ito, O.2
  • 40
    • 0001028296 scopus 로고
    • Picosecond fluorescence studies of rose bengal in aqueous micellar dispersions
    • Rodgers, M. A. J., (1981) Picosecond fluorescence studies of rose bengal in aqueous micellar dispersions. Chem. Phys. Lett. 78, 509-514.
    • (1981) Chem. Phys. Lett. , vol.78 , pp. 509-514
    • Rodgers, M.A.J.1
  • 41
    • 0000284451 scopus 로고
    • Influence of cationic surfactant on the photoprocesses of eosine and rose bengal in aqueous solution
    • Bilski, P., R. Dabestani, and, C. F. Chignell, (1991) Influence of cationic surfactant on the photoprocesses of eosine and rose bengal in aqueous solution. J. Phys. Chem. 95, 5784-5791.
    • (1991) J. Phys. Chem. , vol.95 , pp. 5784-5791
    • Bilski, P.1    Dabestani, R.2    Chignell, C.F.3
  • 42
    • 0041906767 scopus 로고
    • Picosecond studies of rose bengal fluorescence in reverse micellar systems
    • (Edited by E. P. Press), Plenum Press, New York
    • Rodgers, M. A. J., (1984) Picosecond studies of rose bengal fluorescence in reverse micellar systems. In In Reverse Micelles. (Edited by, E. P. Press,), pp. 164-173. Plenum Press, New York.
    • (1984) In Reverse Micelles , pp. 164-173
    • Rodgers, M.A.J.1
  • 43
    • 34250790732 scopus 로고    scopus 로고
    • Binding of rose bengal to bovine serum albumin
    • Abuin, E., A. Aspee, E. Lissi, and, L. Leon, (2007) Binding of rose bengal to bovine serum albumin. J. Chil. Chem. Soc. 52, 1196-1197.
    • (2007) J. Chil. Chem. Soc. , vol.52 , pp. 1196-1197
    • Abuin, E.1    Aspee, A.2    Lissi, E.3    Leon, L.4
  • 44
    • 77953036012 scopus 로고    scopus 로고
    • Surface plasmons control the dynamics of excited triplet states in the presence of gold nanoparticles
    • Pacioni, N. L., M. Gonzalez-Bejar, E. Alarcon, K. L. McGilvray, and, J. C. Scaiano, (2010) Surface plasmons control the dynamics of excited triplet states in the presence of gold nanoparticles. J. Am. Chem. Soc. 132, 6298-6299.
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 6298-6299
    • Pacioni, N.L.1    Gonzalez-Bejar, M.2    Alarcon, E.3    McGilvray, K.L.4    Scaiano, J.C.5
  • 45
    • 34249809404 scopus 로고    scopus 로고
    • Photosensitizing activity of advanced glycation endproducts on tryptophan, glucose 6-phosphate dehydrogenase, human serum albumin and ascorbic acid evaluated at low oxygen pressure
    • Fuenteabla, D., M. Galvez, E. Alarcon, E. A. Lissi, and, E. Silva, (2007) Photosensitizing activity of advanced glycation endproducts on tryptophan, glucose 6-phosphate dehydrogenase, human serum albumin and ascorbic acid evaluated at low oxygen pressure. Photochem. Photobiol. 83, 563-569.
    • (2007) Photochem. Photobiol. , vol.83 , pp. 563-569
    • Fuenteabla, D.1    Galvez, M.2    Alarcon, E.3    Lissi, E.A.4    Silva, E.5
  • 46
    • 0038023149 scopus 로고    scopus 로고
    • Advanced glycation endproducts as uva photosensitizers of tryptophan and ascorbic acid: Consequences for the lens
    • de La Rochette, A., I. S. Birlouez-Aragon, E. Silva, and, P. Morliere, (2003) Advanced glycation endproducts as uva photosensitizers of tryptophan and ascorbic acid: Consequences for the lens. Biochim. Biophys. Acta, 1621, 235-241.
    • (2003) Biochim. Biophys. Acta , vol.1621 , pp. 235-241
    • De La Rochette, A.1    Birlouez-Aragon, I.S.2    Silva, E.3    Morliere, P.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.