메뉴 건너뛰기




Volumn 34, Issue 2-3, 1996, Pages 203-210

Photodynamic crosslinking of proteins. I. Model studies using histidine- and lysine-containing N-(2-hydroxypropyl) methacrylamide copolymers

Author keywords

N (2 hydroxypropyl)methacrylamide copolymer; Photocrosslinking; Photodynamic therapy; Photosensitization

Indexed keywords

AMINO ACID; AMINOCAPROIC ACID DERIVATIVE; COPOLYMER; CYSTEINE; FREE RADICAL; HISTIDINE; METHACRYLIC ACID DERIVATIVE; N (2 HYDROXYPROPYL)METHACRYLAMIDE; ROSE BENGAL; SINGLET OXYGEN; TYROSINE;

EID: 0030199820     PISSN: 10111344     EISSN: None     Source Type: Journal    
DOI: 10.1016/1011-1344(96)07286-7     Document Type: Article
Times cited : (101)

References (29)
  • 1
    • 0000056718 scopus 로고
    • Photosensitized oxidation of biomolecules
    • A.A. Frimer (ed.), CRC Press, Boca Raton, FL
    • 2, Vol. IV, CRC Press, Boca Raton, FL, 1985, pp. 91-143.
    • (1985) 2 , vol.4 , pp. 91-143
    • Straight, R.C.1    Spikes, J.D.2
  • 2
    • 0344447512 scopus 로고
    • Photosensitized cross-linking of proteins to nucleic acids
    • K.C. Smith (ed.), Plenum, New York
    • [2] C. Hélène, Photosensitized cross-linking of proteins to nucleic acids, in K.C. Smith (ed.), Aging, Carcinogenesis, and Radiation Biology, Plenum, New York, 1976, pp. 149-163.
    • (1976) Aging, Carcinogenesis, and Radiation Biology , pp. 149-163
    • Hélène, C.1
  • 3
    • 0028899736 scopus 로고
    • Involvement of H1 and other chromatin proteins in the formation of DNA-protein cross-links induced by visible light in the presence of methylene blue
    • [3] R. Lalwani, S. Maiti and S. Mukherji, Involvement of H1 and other chromatin proteins in the formation of DNA-protein cross-links induced by visible light in the presence of methylene blue, J. Photochem. Photobiol. B: Biol., 27 (1995) 117-122.
    • (1995) J. Photochem. Photobiol. B: Biol. , vol.27 , pp. 117-122
    • Lalwani, R.1    Maiti, S.2    Mukherji, S.3
  • 4
    • 0024064928 scopus 로고
    • Modification of ε-amino group of lysines, cholesterol oxidation and oxidized lipid-apoprotein cross-link formation by porphyrin-photosensitized oxidation of human low density lipoproteins
    • [4] C. Candide, J.P. Reyftmann, R. Santus, J.C. Mazière, P. Morlière and S. Goldstein, Modification of ε-amino group of lysines, cholesterol oxidation and oxidized lipid-apoprotein cross-link formation by porphyrin-photosensitized oxidation of human low density lipoproteins, Photochem. Photobiol., 48 (1988) 137-146.
    • (1988) Photochem. Photobiol. , vol.48 , pp. 137-146
    • Candide, C.1    Reyftmann, J.P.2    Santus, R.3    Mazière, J.C.4    Morlière, P.5    Goldstein, S.6
  • 5
    • 0020457906 scopus 로고
    • Hematoporphyrin-induced photo-oxidation and photodynamic cross-linking of nucleic acids and their constituents
    • [5] T.M.A.R. Dubbelman, A.L. Van Steveninck and J. Van Steveninck, Hematoporphyrin-induced photo-oxidation and photodynamic cross-linking of nucleic acids and their constituents, Biochim. Biophys. Acta, 719 (1982) 47-52.
    • (1982) Biochim. Biophys. Acta , vol.719 , pp. 47-52
    • Dubbelman, T.M.A.R.1    Van Steveninck, A.L.2    Van Steveninck, J.3
  • 6
    • 0018095222 scopus 로고
    • Photodynamic effects of protoporphyrin on human erythrocytes. Nature of the cross-linking of membrane proteins
    • [6] T.M.A.R. Dubbelman, A.F.P.M. De Goeij and J. Van Steveninck, Photodynamic effects of protoporphyrin on human erythrocytes. Nature of the cross-linking of membrane proteins, Biochim. Biophys. Acta, 511 (1978) 141-151.
    • (1978) Biochim. Biophys. Acta , vol.511 , pp. 141-151
    • Dubbelman, T.M.A.R.1    De Goeij, A.F.P.M.2    Van Steveninck, J.3
  • 7
    • 0019327158 scopus 로고
    • Photosensitized cross-linking of erythrocyte membrane proteins. Evidence against participation of amino groups in the reaction
    • [7] A.W. Girotti, Photosensitized cross-linking of erythrocyte membrane proteins. Evidence against participation of amino groups in the reaction, Biochim. Biophys. Acta, 602 (1980) 45-56.
    • (1980) Biochim. Biophys. Acta , vol.602 , pp. 45-56
    • Girotti, A.W.1
  • 8
    • 0018665085 scopus 로고
    • On the mode of cytotoxic action of photoactivated porphyrins
    • [8] K. Kohn and D. Kessel, On the mode of cytotoxic action of photoactivated porphyrins, Biochem. Pharmacol., 28 (1979) 2465-2470.
    • (1979) Biochem. Pharmacol. , vol.28 , pp. 2465-2470
    • Kohn, K.1    Kessel, D.2
  • 9
    • 4243610237 scopus 로고
    • Involvement of imidazole-imidazole and imidazole-sulfhydryl interactions in photodynamic crosslinking of proteins
    • [9] J. Van Steveninck, J. Kögeler and T.M.A.R. Dubbelman, Involvement of imidazole-imidazole and imidazole-sulfhydryl interactions in photodynamic crosslinking of proteins, Biochim. Biophys. Acta, 788 (1984) 35-40.
    • (1984) Biochim. Biophys. Acta , vol.788 , pp. 35-40
    • Van Steveninck, J.1    Kögeler, J.2    Dubbelman, T.M.A.R.3
  • 10
    • 84985451848 scopus 로고
    • Model studies on photodynamic cross-linking
    • [10] H. Verweij and J. Van Steveninck, Model studies on photodynamic cross-linking, Photochem. Photobiol., 35 (1982) 265-267.
    • (1982) Photochem. Photobiol. , vol.35 , pp. 265-267
    • Verweij, H.1    Van Steveninck, J.2
  • 11
    • 0021685159 scopus 로고
    • Photodynamic intramolecular crosslinking of myoglobin
    • [11] J. Van Steveninck and T.M.A.R. Dubbelman, Photodynamic intramolecular crosslinking of myoglobin, Biochim. Biophys. Acta, 791 (1984) 98-101.
    • (1984) Biochim. Biophys. Acta , vol.791 , pp. 98-101
    • Van Steveninck, J.1    Dubbelman, T.M.A.R.2
  • 12
    • 0024337751 scopus 로고
    • A dyephotosensitized reaction that generates stable protein-protein crosslinks
    • [12] A. Webster, D. Britton, A. Apap-Bologna and G. Kemp, A dyephotosensitized reaction that generates stable protein-protein crosslinks, Anal. Biochem., 179 (1989) 154-157.
    • (1989) Anal. Biochem. , vol.179 , pp. 154-157
    • Webster, A.1    Britton, D.2    Apap-Bologna, A.3    Kemp, G.4
  • 15
    • 0001727904 scopus 로고
    • Normal tissue damage following photodynamic therapy: Are there biological advantages?
    • B.W. Henderson and T. J. Dougherty (eds.), Marcel Dekker, New York
    • [15] H. Barr and S.G. Bown, Normal tissue damage following photodynamic therapy: are there biological advantages?, in B.W. Henderson and T. J. Dougherty (eds.), Photodynamic Therapy, Marcel Dekker, New York, 1992, pp. 201-216.
    • (1992) Photodynamic Therapy , pp. 201-216
    • Barr, H.1    Bown, S.G.2
  • 16
    • 49549170184 scopus 로고
    • Poly[N-(2-hydroxypropyl)methacrylamide]. 1. Radical polymerization and copolymerization
    • [16] J. Kopeček and H. Bažilová, Poly[N-(2-hydroxypropyl)methacrylamide]. 1. Radical polymerization and copolymerization, Eur. Polym. J., 9 (1973) 7-14.
    • (1973) Eur. Polym. J. , vol.9 , pp. 7-14
    • Kopeček, J.1    Bažilová, H.2
  • 18
    • 0000932483 scopus 로고
    • Aminolyses of monomeric and polymeric p-nitrophenyl esters of methacryloylated amino acids
    • [18] P. Rejmanová, J. Labský and J. Kopeček, Aminolyses of monomeric and polymeric p-nitrophenyl esters of methacryloylated amino acids, Makromol. Chem., 178 (1971) 2159-2168.
    • (1971) Makromol. Chem. , vol.178 , pp. 2159-2168
    • Rejmanová, P.1    Labský, J.2    Kopeček, J.3
  • 19
    • 0027404146 scopus 로고
    • 6 (NPe6): A candidate sensitizer for the photodynamic therapy of tumors
    • 6 (NPe6): a candidate sensitizer for the photodynamic therapy of tumors, J. Photochem. Photobiol. B: Biol., 17 (1993) 135-143.
    • (1993) J. Photochem. Photobiol. B: Biol. , vol.17 , pp. 135-143
    • Spikes, J.D.1    Bommer, J.C.2
  • 20
    • 0015522277 scopus 로고
    • Fluorescamine: A reagent for assay of amino acids, peptides, and primary amines in the picomole range
    • [20] S. Undenfriend, S. Stein, P. Bohlen, W. Dairman, W. Leimgruberand M. Weigele, Fluorescamine: a reagent for assay of amino acids, peptides, and primary amines in the picomole range, Science, 178 (1972) 871-872.
    • (1972) Science , vol.178 , pp. 871-872
    • Undenfriend, S.1    Stein, S.2    Bohlen, P.3    Dairman, W.4    Leimgruberand, W.5    Weigele, M.6
  • 21
    • 0000184027 scopus 로고
    • Reactive copolymers of N-(2-hydroxypropyl)methacrylamide with N-methacryloylated derivatives of L-leucine and L-phenylalanine. I. Preparation, characterization and reaction with diamines
    • [21] J. Kopecek, Reactive copolymers of N-(2-hydroxypropyl)methacrylamide with N-methacryloylated derivatives of L-leucine and L-phenylalanine. I. Preparation, characterization and reaction with diamines, Makromol. Chem., 178 (1977) 2169-2183.
    • (1977) Makromol. Chem. , vol.178 , pp. 2169-2183
    • Kopecek, J.1
  • 22
    • 0010755501 scopus 로고
    • Theory of molecular size distribution and gel formation in branched polymers. II. General crosslinking
    • [22] W.H. Stockmeyer, Theory of molecular size distribution and gel formation in branched polymers. II. General crosslinking, J. Chem. Phys., 12 (1944) 125-131.
    • (1944) J. Chem. Phys. , vol.12 , pp. 125-131
    • Stockmeyer, W.H.1
  • 23
    • 0001937522 scopus 로고
    • Photosensitization
    • K.C. Smith (ed.), Plenum, New York, 2nd edn.
    • [23] J.D. Spikes, Photosensitization, in K.C. Smith (ed.), The Science of Photobiology, Plenum, New York, 2nd edn., 1989, pp. 79-110.
    • (1989) The Science of Photobiology , pp. 79-110
    • Spikes, J.D.1
  • 25
    • 0028391073 scopus 로고
    • Reactivity of singlet oxygen toward amino acids and peptides
    • [25] A. Michaeli and J. Feitelson, Reactivity of singlet oxygen toward amino acids and peptides, Photochem. Photobiol., 59 (1994) 284-289.
    • (1994) Photochem. Photobiol. , vol.59 , pp. 284-289
    • Michaeli, A.1    Feitelson, J.2
  • 26
    • 0029262620 scopus 로고
    • Reactivity of singlet oxygen toward large peptides
    • [26] A. Michaeli and J. Feitelson, Reactivity of singlet oxygen toward large peptides, Photochem. Photobiol., 61 (1995) 255-260.
    • (1995) Photochem. Photobiol. , vol.61 , pp. 255-260
    • Michaeli, A.1    Feitelson, J.2
  • 29
    • 0001781841 scopus 로고
    • Synthesis of tailor-made soluble polymeric drug carriers
    • J.M. Anderson and S.W. Kim (eds.), Plenum, New York
    • [29] J. Kopeček, Synthesis of tailor-made soluble polymeric drug carriers, in J.M. Anderson and S.W. Kim (eds.), Recent Advances in Drug Delivery Systems, Plenum, New York, 1984, pp. 41-62.
    • (1984) Recent Advances in Drug Delivery Systems , pp. 41-62
    • Kopeček, J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.