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Volumn 147, Issue 3, 2010, Pages 111-122

Human serum albumin binding ibuprofen: A 3D description of the unfolding pathway in urea

Author keywords

Ab initio calculation (reconstruction); Antidenaturant effect; Human serum albumin; Protein unfolding; Singular value decomposition method; Small angle X ray scattering

Indexed keywords

HUMAN SERUM ALBUMIN; IBUPROFEN; UREA;

EID: 77649338894     PISSN: 03014622     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bpc.2010.01.002     Document Type: Article
Times cited : (41)

References (61)
  • 1
    • 33947465045 scopus 로고
    • The interaction of human serum in albumin with long-chain fatty acid anions
    • Goodman D.S. The interaction of human serum in albumin with long-chain fatty acid anions. J. Am. Chem. Soc. 80 (1958) 3892-3898
    • (1958) J. Am. Chem. Soc. , vol.80 , pp. 3892-3898
    • Goodman, D.S.1
  • 2
    • 0016801988 scopus 로고
    • The characterization of two specific drug binding sites on human serum albumin
    • Sudlow G., Birkett D.J., and Wade D.N. The characterization of two specific drug binding sites on human serum albumin. Mol. Pharmacol. 11 (1975) 824-832
    • (1975) Mol. Pharmacol. , vol.11 , pp. 824-832
    • Sudlow, G.1    Birkett, D.J.2    Wade, D.N.3
  • 3
    • 0017174391 scopus 로고
    • Further characterization of specific drug binding sites on human serum albumin
    • Sudlow G., Birkett D.J., and Wade D.N. Further characterization of specific drug binding sites on human serum albumin. Mol. Pharmacol. 12 (1976) 1052-1061
    • (1976) Mol. Pharmacol. , vol.12 , pp. 1052-1061
    • Sudlow, G.1    Birkett, D.J.2    Wade, D.N.3
  • 5
    • 0018397880 scopus 로고
    • Characterization of a specific drug binding site of human serum albumin. Means. Characterization of a specific drug binding site of human serum albumin
    • Sollene N.P., and Means G.E. Characterization of a specific drug binding site of human serum albumin. Means. Characterization of a specific drug binding site of human serum albumin. Mol. Pharmacol. 14 (1979) 754-757
    • (1979) Mol. Pharmacol. , vol.14 , pp. 754-757
    • Sollene, N.P.1    Means, G.E.2
  • 6
    • 0019171647 scopus 로고
    • Effects of drug binding on the esterase activity of human serum albumin: inhibition modes and binding sites of anionic drugs
    • Ozeki Y., Kurono Y., Yotsuyanagi T., and Ikeda K. Effects of drug binding on the esterase activity of human serum albumin: inhibition modes and binding sites of anionic drugs. Chem. Pharmacol. Bull. 28 (1980) 535-540
    • (1980) Chem. Pharmacol. Bull. , vol.28 , pp. 535-540
    • Ozeki, Y.1    Kurono, Y.2    Yotsuyanagi, T.3    Ikeda, K.4
  • 7
    • 0023151449 scopus 로고
    • Effects of drug bindings on the esterase-like activity of human serum albumin. VII. Subdivision of R-type drugs inhibiting the activity towards p-nitrophenyl acetate
    • Kurono Y., Ozeki Y., Yamada H., Takeuchi T., and Ikeda K. Effects of drug bindings on the esterase-like activity of human serum albumin. VII. Subdivision of R-type drugs inhibiting the activity towards p-nitrophenyl acetate. Chem. Pharmacol. Bull. 35 (1987) 734-739
    • (1987) Chem. Pharmacol. Bull. , vol.35 , pp. 734-739
    • Kurono, Y.1    Ozeki, Y.2    Yamada, H.3    Takeuchi, T.4    Ikeda, K.5
  • 8
    • 0020660621 scopus 로고
    • Relations between high-affinity binding sites for l-tryptophan, diazepam, salicylate and phenol red on human serum albumin
    • Kragh-Hansen U. Relations between high-affinity binding sites for l-tryptophan, diazepam, salicylate and phenol red on human serum albumin. Biochem. J. 209 (1983) 135-142
    • (1983) Biochem. J. , vol.209 , pp. 135-142
    • Kragh-Hansen, U.1
  • 9
    • 0021984733 scopus 로고
    • Relations between high-affinity binding sites of markers for binding regions on human serum albumin
    • Kragh-Hansen U. Relations between high-affinity binding sites of markers for binding regions on human serum albumin. Biochem. J. 225 (1985) 629-638
    • (1985) Biochem. J. , vol.225 , pp. 629-638
    • Kragh-Hansen, U.1
  • 10
    • 0023688913 scopus 로고
    • Evidence for a large and flexible region of human serum albumin possessing high affinity binding sites for salicylate, warfarin, and other ligands
    • Kragh-Hansen U. Evidence for a large and flexible region of human serum albumin possessing high affinity binding sites for salicylate, warfarin, and other ligands. Mol. Pharmacol. 34 (1988) 160-171
    • (1988) Mol. Pharmacol. , vol.34 , pp. 160-171
    • Kragh-Hansen, U.1
  • 11
    • 0030592163 scopus 로고    scopus 로고
    • Characterization of site I on human serum albumin: concept about the structure of a drug binding site
    • Yamasaki K., Maruyama T., Kragh-Hansen U., and Otagiri M. Characterization of site I on human serum albumin: concept about the structure of a drug binding site. Biochim. Biophys. Acta 1295 (1996) 147-157
    • (1996) Biochim. Biophys. Acta , vol.1295 , pp. 147-157
    • Yamasaki, K.1    Maruyama, T.2    Kragh-Hansen, U.3    Otagiri, M.4
  • 12
    • 0030701947 scopus 로고    scopus 로고
    • Stereoselectivity and enantiomer-enantiomer interactions in the binding of ibuprofen to human serum albumin
    • Itoh T., Suara Y., Tsuda Y., and Yamada H. Stereoselectivity and enantiomer-enantiomer interactions in the binding of ibuprofen to human serum albumin. Chirality 9 (1997) 643-649
    • (1997) Chirality , vol.9 , pp. 643-649
    • Itoh, T.1    Suara, Y.2    Tsuda, Y.3    Yamada, H.4
  • 13
    • 14544296120 scopus 로고    scopus 로고
    • Protein binding study of S-ibuprofen using high-performance frontal analysis
    • Jin L., Choi D.Y., Liu H., and Row R.H. Protein binding study of S-ibuprofen using high-performance frontal analysis. Bull. Korean Chem. Soc. 26 (2005) 136-138
    • (2005) Bull. Korean Chem. Soc. , vol.26 , pp. 136-138
    • Jin, L.1    Choi, D.Y.2    Liu, H.3    Row, R.H.4
  • 14
    • 51349131362 scopus 로고    scopus 로고
    • Ibuprofen induces an allosteric conformational transition in the heme complex of human serum albumin with significant effects on heme ligation
    • Nicoletti F.P., Howes B.D., Fittipaldi M., Fanali G., Fasano M., Ascenzi P., and Smulevich G. Ibuprofen induces an allosteric conformational transition in the heme complex of human serum albumin with significant effects on heme ligation. J. Am. Chem. Soc. 130 (2008) 11677-11688
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 11677-11688
    • Nicoletti, F.P.1    Howes, B.D.2    Fittipaldi, M.3    Fanali, G.4    Fasano, M.5    Ascenzi, P.6    Smulevich, G.7
  • 16
    • 0032967544 scopus 로고    scopus 로고
    • Inhibition of protein denaturation by fatty acids, bile salts and other natural substances: a new hypothesis for the mechanism of action of fish oil in rheumatic diseases
    • Saso L., Valentini G., Casini M.L., Mattei E., Braghiroli L., Mazzanti G., Panzironi C., Grippa E., and Silvestrini B. Inhibition of protein denaturation by fatty acids, bile salts and other natural substances: a new hypothesis for the mechanism of action of fish oil in rheumatic diseases. Jpn. J. Pharmacol. 79 (1999) 89-99
    • (1999) Jpn. J. Pharmacol. , vol.79 , pp. 89-99
    • Saso, L.1    Valentini, G.2    Casini, M.L.3    Mattei, E.4    Braghiroli, L.5    Mazzanti, G.6    Panzironi, C.7    Grippa, E.8    Silvestrini, B.9
  • 18
    • 28844473250 scopus 로고    scopus 로고
    • Unfolding pathways of human serum albumin: evidence for sequential unfolding and folding of its three domains
    • Santra M.K., Banerjee A., Rahaman O., and Panda D. Unfolding pathways of human serum albumin: evidence for sequential unfolding and folding of its three domains. Int. J. Biol. Macromol. 37 (2005) 200-204
    • (2005) Int. J. Biol. Macromol. , vol.37 , pp. 200-204
    • Santra, M.K.1    Banerjee, A.2    Rahaman, O.3    Panda, D.4
  • 19
    • 33750833403 scopus 로고    scopus 로고
    • Conformational study of human serum albumin in pre-denaturation temperatures by differential scanning calorimetry, circular dichroism and UV spectroscopy
    • Rezaei-Tavirani M., Moghaddamnia S.H., Ranjbar B., Amani M., and Marashi S.A. Conformational study of human serum albumin in pre-denaturation temperatures by differential scanning calorimetry, circular dichroism and UV spectroscopy. J. Biochem. Mol. Biol. 39 (2006) 530-536
    • (2006) J. Biochem. Mol. Biol. , vol.39 , pp. 530-536
    • Rezaei-Tavirani, M.1    Moghaddamnia, S.H.2    Ranjbar, B.3    Amani, M.4    Marashi, S.A.5
  • 21
    • 70349132068 scopus 로고    scopus 로고
    • Urea-induced denaturation process on defatted human serum albumin and in the presence of palmitic acid
    • Leggio C., Galantini L., Konarev P.V., and Pavel N.V. Urea-induced denaturation process on defatted human serum albumin and in the presence of palmitic acid. J. Phys. Chem. B 113 (2009) 12590-12602
    • (2009) J. Phys. Chem. B , vol.113 , pp. 12590-12602
    • Leggio, C.1    Galantini, L.2    Konarev, P.V.3    Pavel, N.V.4
  • 22
    • 0028871804 scopus 로고
    • How to measure and predict the molar absorption coefficient of a protein
    • Pace C.N., Vajdos F., Fee L., Grimsley G., and Gray T. How to measure and predict the molar absorption coefficient of a protein. Protein Sci. 4 (1995) 2411-2423
    • (1995) Protein Sci. , vol.4 , pp. 2411-2423
    • Pace, C.N.1    Vajdos, F.2    Fee, L.3    Grimsley, G.4    Gray, T.5
  • 23
    • 0015522150 scopus 로고
    • Determination of the secondary structures of proteins by circular dichroism and optical rotatory dispersion
    • Chen Y.H., Yang J.T., and Martinez H.M. Determination of the secondary structures of proteins by circular dichroism and optical rotatory dispersion. Biochemistry 11 (1972) 4120-4131
    • (1972) Biochemistry , vol.11 , pp. 4120-4131
    • Chen, Y.H.1    Yang, J.T.2    Martinez, H.M.3
  • 27
    • 0000323953 scopus 로고
    • For the measurement of the absolute intensity of X-ray small angle scattering, the moving slit method
    • Stabinger H., Kratky O., and New Technique A. For the measurement of the absolute intensity of X-ray small angle scattering, the moving slit method. Makromol. Chem. 179 (1978) 1655-1659
    • (1978) Makromol. Chem. , vol.179 , pp. 1655-1659
    • Stabinger, H.1    Kratky, O.2    New Technique, A.3
  • 29
    • 0034484513 scopus 로고    scopus 로고
    • SAXS experiments on absolute scale with Kratky systems using water as a secondary standard
    • Orthaber D., Bergmann A., and Glatter O. SAXS experiments on absolute scale with Kratky systems using water as a secondary standard. J. Appl. Crystallogr. 33 (2000) 218-225
    • (2000) J. Appl. Crystallogr. , vol.33 , pp. 218-225
    • Orthaber, D.1    Bergmann, A.2    Glatter, O.3
  • 30
    • 0000897622 scopus 로고
    • A new method for the evaluation of small-angle scattering data
    • Glatter O. A new method for the evaluation of small-angle scattering data. J. Appl. Crystallogr. 10 (1977) 415-421
    • (1977) J. Appl. Crystallogr. , vol.10 , pp. 415-421
    • Glatter, O.1
  • 32
    • 0030572626 scopus 로고    scopus 로고
    • A lysozyme folding intermediate revealed by solution X-ray scattering
    • Chen L., Hodgson K.O., and Doniach S. A lysozyme folding intermediate revealed by solution X-ray scattering. J. Mol. Biol. 261 (1996) 658-671
    • (1996) J. Mol. Biol. , vol.261 , pp. 658-671
    • Chen, L.1    Hodgson, K.O.2    Doniach, S.3
  • 33
    • 0042820143 scopus 로고    scopus 로고
    • Further insights into calmodulin-myosin light chain kinase interaction from solution scattering and shape restoration
    • Heller W.T., Krueger J.K., and Trewhella J. Further insights into calmodulin-myosin light chain kinase interaction from solution scattering and shape restoration. Biochemistry 42 (2003) 10579-10588
    • (2003) Biochemistry , vol.42 , pp. 10579-10588
    • Heller, W.T.1    Krueger, J.K.2    Trewhella, J.3
  • 34
    • 21644489425 scopus 로고    scopus 로고
    • Influence of multiple well defined conformations on small-angle scattering of proteins in solution
    • Heller W.T. Influence of multiple well defined conformations on small-angle scattering of proteins in solution. Acta Crystallogr. D61 (2005) 33-44
    • (2005) Acta Crystallogr. , vol.D61 , pp. 33-44
    • Heller, W.T.1
  • 35
    • 23244455562 scopus 로고    scopus 로고
    • Global rigid body modeling of macromolecular complexes against small-angle scattering data
    • Petoukhov M.V., and Svergun D.I. Global rigid body modeling of macromolecular complexes against small-angle scattering data. Biophys. J. 89 (2005) 1237-1250
    • (2005) Biophys. J. , vol.89 , pp. 1237-1250
    • Petoukhov, M.V.1    Svergun, D.I.2
  • 36
    • 0029185933 scopus 로고
    • CRYSOL - a program to evaluate X-ray solution scattering of biological macromolecules from atomic coordinates
    • Svergun D.I., Barberato C., and Koch M.H.J. CRYSOL - a program to evaluate X-ray solution scattering of biological macromolecules from atomic coordinates. J. Appl. Crystallogr. 28 (1995) 768-773
    • (1995) J. Appl. Crystallogr. , vol.28 , pp. 768-773
    • Svergun, D.I.1    Barberato, C.2    Koch, M.H.J.3
  • 37
    • 33847041091 scopus 로고    scopus 로고
    • Comment on the misunderstanding of the BSA-SDS complex model: concern about publications of an impractical model
    • Takeda K., and Moriyama Y. Comment on the misunderstanding of the BSA-SDS complex model: concern about publications of an impractical model. J. Phys. Chem. B. 111 (2007) 1244
    • (2007) J. Phys. Chem. B. , vol.111 , pp. 1244
    • Takeda, K.1    Moriyama, Y.2
  • 40
    • 0035124442 scopus 로고    scopus 로고
    • A software system for rigid body modeling of solution scattering data
    • Kozin M.B., and Svergun D.I. A software system for rigid body modeling of solution scattering data. J. Appl. Crystallogr. 34 (2001) 33-41
    • (2001) J. Appl. Crystallogr. , vol.34 , pp. 33-41
    • Kozin, M.B.1    Svergun, D.I.2
  • 41
    • 0001229341 scopus 로고    scopus 로고
    • Calculation of hydrodynamic properties of globular proteins from their atomic-level structure
    • García de la Torre J., Huertas M.L., and Carrasco B. Calculation of hydrodynamic properties of globular proteins from their atomic-level structure. Biophys. J. 78 (2000) 719-730
    • (2000) Biophys. J. , vol.78 , pp. 719-730
    • García de la Torre, J.1    Huertas, M.L.2    Carrasco, B.3
  • 42
    • 0033039369 scopus 로고    scopus 로고
    • Hydrodynamic properties of rigid particles: comparison of different modeling and computational procedures
    • Carrasco B., and García de la Torre J. Hydrodynamic properties of rigid particles: comparison of different modeling and computational procedures. Biophys. J. 76 (1999) 3044-3057
    • (1999) Biophys. J. , vol.76 , pp. 3044-3057
    • Carrasco, B.1    García de la Torre, J.2
  • 43
    • 52649126204 scopus 로고    scopus 로고
    • Urea-induced denaturation of human serum albumin labeled with acrylodan
    • González-Jiménez J., and Cortijo M. Urea-induced denaturation of human serum albumin labeled with acrylodan. J Prot. Chem. 21 (2002) 75-79
    • (2002) J Prot. Chem. , vol.21 , pp. 75-79
    • González-Jiménez, J.1    Cortijo, M.2
  • 44
    • 2442444146 scopus 로고    scopus 로고
    • Effect of urea on bovine serum albumin in aqueous and reverse micelle environments investigated by small angle X-ray scattering, fluorescence and circular dichroism
    • Itri R., Caetano W., Barbosa L.R.S., and Baptista M.S. Effect of urea on bovine serum albumin in aqueous and reverse micelle environments investigated by small angle X-ray scattering, fluorescence and circular dichroism. Braz. J. Phys. 34 (2004) 58-63
    • (2004) Braz. J. Phys. , vol.34 , pp. 58-63
    • Itri, R.1    Caetano, W.2    Barbosa, L.R.S.3    Baptista, M.S.4
  • 45
    • 23244452958 scopus 로고    scopus 로고
    • Effect of urea on peptide conformation in water: molecular dynamics and experimental characterization
    • Caballero-Herrera A., Nordstrand K., Bernt K.D., and Nilsson L. Effect of urea on peptide conformation in water: molecular dynamics and experimental characterization. Biophys. J. 89 (2005) 842-857
    • (2005) Biophys. J. , vol.89 , pp. 842-857
    • Caballero-Herrera, A.1    Nordstrand, K.2    Bernt, K.D.3    Nilsson, L.4
  • 46
    • 11344259541 scopus 로고    scopus 로고
    • Characterization of the denaturation of human α-lactalbumin in urea by molecular dynamics simulations
    • Smith L.J., Jones R.M., and Gunsteren W.F. Characterization of the denaturation of human α-lactalbumin in urea by molecular dynamics simulations. Proteins 58 (2005) 439-449
    • (2005) Proteins , vol.58 , pp. 439-449
    • Smith, L.J.1    Jones, R.M.2    Gunsteren, W.F.3
  • 47
    • 55949131241 scopus 로고    scopus 로고
    • Urea denaturation by stronger dispersion interactions with proteins than water implies a 2-stage unfolding
    • Hua L., Zhou R., Thirumalai D., and Berne B.J. Urea denaturation by stronger dispersion interactions with proteins than water implies a 2-stage unfolding. Proc. Natl. Acad. Sci. 105 (2008) 16928-16933
    • (2008) Proc. Natl. Acad. Sci. , vol.105 , pp. 16928-16933
    • Hua, L.1    Zhou, R.2    Thirumalai, D.3    Berne, B.J.4
  • 48
    • 0015424902 scopus 로고
    • A comparison of X-ray small-angle scattering results to crystal structure analysis and other physical techniques in the field of biological macromolecules
    • Kratky O., and Pilz I. A comparison of X-ray small-angle scattering results to crystal structure analysis and other physical techniques in the field of biological macromolecules. Q. Rev. Biophys. 5 (1972) 481-537
    • (1972) Q. Rev. Biophys. , vol.5 , pp. 481-537
    • Kratky, O.1    Pilz, I.2
  • 49
    • 0032497321 scopus 로고    scopus 로고
    • A small-angle X-ray scattering study of the ensemble of unfolded states of cytochrome c
    • Segel D.J., Fink A.L., Hodgson K.O., and Doniach S. A small-angle X-ray scattering study of the ensemble of unfolded states of cytochrome c. Biochemistry 37 (1998) 12443-12451
    • (1998) Biochemistry , vol.37 , pp. 12443-12451
    • Segel, D.J.1    Fink, A.L.2    Hodgson, K.O.3    Doniach, S.4
  • 50
    • 0033532201 scopus 로고    scopus 로고
    • Characterization of transient intermediates in lysozyme folding with time-resolved small-angle X-ray scattering
    • Segel D.J., Bachmann A., Hofrichter J., Hodgson K.O., Doniach S., and Kiefhaber T. Characterization of transient intermediates in lysozyme folding with time-resolved small-angle X-ray scattering. J. Mol. Biol. 288 (1999) 489-499
    • (1999) J. Mol. Biol. , vol.288 , pp. 489-499
    • Segel, D.J.1    Bachmann, A.2    Hofrichter, J.3    Hodgson, K.O.4    Doniach, S.5    Kiefhaber, T.6
  • 51
    • 0034237709 scopus 로고    scopus 로고
    • Anion-induced stabilization of human serum albumin prevents the formation of intermediate during denaturation
    • Muzammil S., Kumar Y., and Tayyab S. Anion-induced stabilization of human serum albumin prevents the formation of intermediate during denaturation. Proteins 40 (2000) 29-38
    • (2000) Proteins , vol.40 , pp. 29-38
    • Muzammil, S.1    Kumar, Y.2    Tayyab, S.3
  • 52
    • 0022555885 scopus 로고
    • Denaturation and analysis of urea and guanidine hydrochloride denaturation curves
    • Pace C.N. Denaturation and analysis of urea and guanidine hydrochloride denaturation curves. Methods Enzymol. 131 (1986) 266-279
    • (1986) Methods Enzymol. , vol.131 , pp. 266-279
    • Pace, C.N.1
  • 53
    • 56349119329 scopus 로고    scopus 로고
    • About the albumin structure in solution: cigar Expanded form versus heart Normal shape
    • Leggio C., Galantini L., and Pavel N.V. About the albumin structure in solution: cigar Expanded form versus heart Normal shape. Phys. Chem. Chem. Phys. 10 (2008) 6741-6750
    • (2008) Phys. Chem. Chem. Phys. , vol.10 , pp. 6741-6750
    • Leggio, C.1    Galantini, L.2    Pavel, N.V.3
  • 54
    • 57949110254 scopus 로고    scopus 로고
    • Human Serum Albumin Unfolding: A Small-Angle X-ray Scattering and Light Scattering Study
    • Galantini L., Leggio C., and Pavel N.V. Human Serum Albumin Unfolding: A Small-Angle X-ray Scattering and Light Scattering Study. J. Phys. Chem. B 112 (2008) 15460-15469
    • (2008) J. Phys. Chem. B , vol.112 , pp. 15460-15469
    • Galantini, L.1    Leggio, C.2    Pavel, N.V.3
  • 55
    • 33847119938 scopus 로고    scopus 로고
    • Protein Interactions Studied by SAXS: Effect of Ionic Strength and Protein Concentration for BSA in Aqueous Solutions
    • Zhang F., Skoda M.W.A., Jacobs R.M.J., Martin R.A., Martin C.M., and Schreiber F. Protein Interactions Studied by SAXS: Effect of Ionic Strength and Protein Concentration for BSA in Aqueous Solutions. J. Phys. Chem. B 111 (2007) 251-259
    • (2007) J. Phys. Chem. B , vol.111 , pp. 251-259
    • Zhang, F.1    Skoda, M.W.A.2    Jacobs, R.M.J.3    Martin, R.A.4    Martin, C.M.5    Schreiber, F.6
  • 56
    • 0034299210 scopus 로고    scopus 로고
    • Study on Intermicellar Interactions and Micellar Size in Aqueous Solutions of NaTDC by Measurements of Collective Diffusion and Self-Diffusion Coefficients
    • D'Archivio A.A., Galantini L., and Tettamanti E. Study on Intermicellar Interactions and Micellar Size in Aqueous Solutions of NaTDC by Measurements of Collective Diffusion and Self-Diffusion Coefficients. J. Phys. Chem. B 104 (2000) 9255-9259
    • (2000) J. Phys. Chem. B , vol.104 , pp. 9255-9259
    • D'Archivio, A.A.1    Galantini, L.2    Tettamanti, E.3
  • 57
    • 0038408836 scopus 로고    scopus 로고
    • Effect of urea on serum albumin complex with antithyroid drugs: fluorescence study
    • Sulkowska A., Bojko B., Rownicka J., Pentak D., and Sulkowski W. Effect of urea on serum albumin complex with antithyroid drugs: fluorescence study. J. Mol. Struct. 651 (2003) 237
    • (2003) J. Mol. Struct. , vol.651 , pp. 237
    • Sulkowska, A.1    Bojko, B.2    Rownicka, J.3    Pentak, D.4    Sulkowski, W.5
  • 58
    • 33947644936 scopus 로고    scopus 로고
    • Binding Interaction of a Biological Photosensitizer with Serum Albumins: A Biophysical Study
    • Chakrabarty A., Mallick A., Haldar B., Das P., and Chattopadhyay N. Binding Interaction of a Biological Photosensitizer with Serum Albumins: A Biophysical Study. Biomacromolecules 8 (2007) 920-927
    • (2007) Biomacromolecules , vol.8 , pp. 920-927
    • Chakrabarty, A.1    Mallick, A.2    Haldar, B.3    Das, P.4    Chattopadhyay, N.5
  • 60
    • 37049034294 scopus 로고    scopus 로고
    • Urea orientation at protein surfaces
    • Chen X X., Sagle L.B., and Cremer P.S. Urea orientation at protein surfaces. J. Am. Chem. Soc. 129 (2007) 15104-15105
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 15104-15105
    • Chen X, X.1    Sagle, L.B.2    Cremer, P.S.3
  • 61
    • 0029051467 scopus 로고
    • Stereospecific and competitive binding of drugs to human serum albumin: a difference circular dichroism approach
    • Ascoli G., Bertucci C., and Salvadori P. Stereospecific and competitive binding of drugs to human serum albumin: a difference circular dichroism approach. J. Pharm. Sci. 84 (1995) 737-741
    • (1995) J. Pharm. Sci. , vol.84 , pp. 737-741
    • Ascoli, G.1    Bertucci, C.2    Salvadori, P.3


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