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Volumn 30, Issue 19, 2014, Pages 5536-5544

Interaction of a hydrophobic-functionalized pamam dendrimer with bovine serum albumin: Thermodynamic and structural changes

Author keywords

[No Author keywords available]

Indexed keywords

BODY FLUIDS; HYDROGEN BONDS; HYDROPHOBICITY; MAMMALS; SPECTROSCOPIC ANALYSIS;

EID: 84900992924     PISSN: 07437463     EISSN: 15205827     Source Type: Journal    
DOI: 10.1021/la501129y     Document Type: Article
Times cited : (55)

References (42)
  • 1
    • 77955579970 scopus 로고    scopus 로고
    • PEGylated polyamidoamine dendrimers with bis-aryl hydrazone linkages for enhanced gene delivery
    • Yuan, Q.; Yeudall, W. A.; Yang, Y. PEGylated polyamidoamine dendrimers with bis-aryl hydrazone linkages for enhanced gene delivery Biomacromolecules 2010, 1, 1940-1947
    • (2010) Biomacromolecules , vol.1 , pp. 1940-1947
    • Yuan, Q.1    Yeudall, W.A.2    Yang, Y.3
  • 2
    • 77954561366 scopus 로고    scopus 로고
    • Interactions between DNA and poly(amido amine) dendrimers on silica surfaces
    • Ainalem, M. L.; Campbell, R. A.; Nylander, T. Interactions between DNA and poly(amido amine) dendrimers on silica surfaces Langmuir 2010, 26, 8625-8635
    • (2010) Langmuir , vol.26 , pp. 8625-8635
    • Ainalem, M.L.1    Campbell, R.A.2    Nylander, T.3
  • 3
    • 65249141045 scopus 로고    scopus 로고
    • Polyamidoamine dendrimers with a modified pentaerythritol core having high efficiency and low cytotoxicity as gene carriers
    • Wang, Y.; Kong, W.; Song, Y.; Duan, Y.; Wang, L.; Steinhoff, G.; Kong, D.; Yu, Y. Polyamidoamine dendrimers with a modified pentaerythritol core having high efficiency and low cytotoxicity as gene carriers Biomacromolecules 2009, 10, 617-622
    • (2009) Biomacromolecules , vol.10 , pp. 617-622
    • Wang, Y.1    Kong, W.2    Song, Y.3    Duan, Y.4    Wang, L.5    Steinhoff, G.6    Kong, D.7    Yu, Y.8
  • 4
    • 0344494597 scopus 로고    scopus 로고
    • Polyplexes assembled with internally quaternized PAMAM-OH dendrimer and plasmid DNA have a neutral surface and gene delivery potency
    • Lee, J. H.; Lim, Y. B.; Choi, J. S.; Lee, Y.; Kim, T.; Kim, H. J.; Yoon, J. K.; Kim, K.; Park, J. S. Polyplexes assembled with internally quaternized PAMAM-OH dendrimer and plasmid DNA have a neutral surface and gene delivery potency Bioconjugate Chem. 2003, 14, 1214-1221
    • (2003) Bioconjugate Chem. , vol.14 , pp. 1214-1221
    • Lee, J.H.1    Lim, Y.B.2    Choi, J.S.3    Lee, Y.4    Kim, T.5    Kim, H.J.6    Yoon, J.K.7    Kim, K.8    Park, J.S.9
  • 5
    • 79952972079 scopus 로고    scopus 로고
    • Multifunctional triblock nanocarrier (PAMAM-PEG-PLL) for the efficient intracellular siRNA delivery and gene silencing
    • Patil, M. L.; Zhang, M.; Minko, T. Multifunctional triblock nanocarrier (PAMAM-PEG-PLL) for the efficient intracellular siRNA delivery and gene silencing ACS Nano 2011, 5, 1877-1887
    • (2011) ACS Nano , vol.5 , pp. 1877-1887
    • Patil, M.L.1    Zhang, M.2    Minko, T.3
  • 8
    • 33745745741 scopus 로고    scopus 로고
    • Thermosensitive properties of poly(amidoamine) dendrimers with peripheral phenylalanine residues
    • Tono, Y.; Kojima, C.; Haba, Y.; Takahashi, T.; Harada, A.; Yagi, S.; Kono, K. Thermosensitive properties of poly(amidoamine) dendrimers with peripheral phenylalanine residues Langmuir 2006, 22, 4920-4922
    • (2006) Langmuir , vol.22 , pp. 4920-4922
    • Tono, Y.1    Kojima, C.2    Haba, Y.3    Takahashi, T.4    Harada, A.5    Yagi, S.6    Kono, K.7
  • 9
    • 0035989698 scopus 로고    scopus 로고
    • Interactions between dendrimer biocides and bacterial membranes
    • Chen, C. Z.; Cooper, S. L. Interactions between dendrimer biocides and bacterial membranes Biomaterials 2002, 23, 3359-3368
    • (2002) Biomaterials , vol.23 , pp. 3359-3368
    • Chen, C.Z.1    Cooper, S.L.2
  • 10
    • 84884476065 scopus 로고    scopus 로고
    • The influence of PAMAM dendrimers surface groups on their interaction with porcine pepsin
    • Ciolkowski, M.; Rozanek, M.; Bryszewska, M.; Klajnert, B. The influence of PAMAM dendrimers surface groups on their interaction with porcine pepsin Biochim. Biophys. Acta 2013, 1834, 1982-1987
    • (2013) Biochim. Biophys. Acta , vol.1834 , pp. 1982-1987
    • Ciolkowski, M.1    Rozanek, M.2    Bryszewska, M.3    Klajnert, B.4
  • 12
    • 80052922757 scopus 로고    scopus 로고
    • Interaction of polyamidoamine (PAMAM) succinamic acid dendrimers generation 4 with human serum albumin
    • Sekowski, S.; Buczkowski, A.; Palecz, B.; Gabryelak, T. Interaction of polyamidoamine (PAMAM) succinamic acid dendrimers generation 4 with human serum albumin Spectrochim. Acta Part A 2011, 81, 706-710
    • (2011) Spectrochim. Acta Part A , vol.81 , pp. 706-710
    • Sekowski, S.1    Buczkowski, A.2    Palecz, B.3    Gabryelak, T.4
  • 13
    • 0026664548 scopus 로고
    • Atomic structure and chemistry of human serum albumin
    • He, X. M.; Carter, D. C. Atomic structure and chemistry of human serum albumin Nature 1992, 358, 209-215
    • (1992) Nature , vol.358 , pp. 209-215
    • He, X.M.1    Carter, D.C.2
  • 17
    • 84884150984 scopus 로고    scopus 로고
    • Contribution of hydrophobicity, DNA and proteins to the cytotoxicity of cationic PAMAM dendrimers
    • Halets, l.; Shcharbin, D.; Klajnert, B.; Bryszewska, M. Contribution of hydrophobicity, DNA and proteins to the cytotoxicity of cationic PAMAM dendrimers Int. J. Pharm. 2013, 454, 1-3
    • (2013) Int. J. Pharm. , vol.454 , pp. 1-3
    • Halets, L.1    Shcharbin, D.2    Klajnert, B.3    Bryszewska, M.4
  • 18
    • 84901040680 scopus 로고    scopus 로고
    • http://www.photophysics.com/software/global-3-analysis-software.
  • 19
    • 84901040671 scopus 로고    scopus 로고
    • http://www.scripps.edu/mb/olson/doc/autodock.
  • 20
    • 84901040672 scopus 로고    scopus 로고
    • http://www.rcsb.org/pdb/explore.do?structureId=3V03.
  • 22
    • 84901040662 scopus 로고    scopus 로고
    • http://www.clcbio.com/products/molgro/.
  • 23
    • 0030579816 scopus 로고    scopus 로고
    • The fluorescence and circular dichroism of proteins in reverse micelles: Application to the photophysics of human serum albumin and N-acetyl- tryptophanamide
    • Davis, D. M.; McLoskey, D.; Birch, D. J. S.; Gellert, P. R.; Kittlety, R. S.; Swart, R. M. The fluorescence and circular dichroism of proteins in reverse micelles: application to the photophysics of human serum albumin and N-acetyl-tryptophanamide Biophys. Chem. 1996, 60, 63-77
    • (1996) Biophys. Chem. , vol.60 , pp. 63-77
    • Davis, D.M.1    McLoskey, D.2    Birch, D.J.S.3    Gellert, P.R.4    Kittlety, R.S.5    Swart, R.M.6
  • 24
    • 35148874214 scopus 로고    scopus 로고
    • Hydration in protein folding: Thermal unfolding/refolding of human serum albumin
    • Mitra, R. K.; Sinha, S. S.; Pal, S. K. Hydration in protein folding: thermal unfolding/refolding of human serum albumin Langmuir 2007, 23, 10224-10229
    • (2007) Langmuir , vol.23 , pp. 10224-10229
    • Mitra, R.K.1    Sinha, S.S.2    Pal, S.K.3
  • 25
    • 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.; Marash, 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. 2006, 39, 530-553
    • (2006) J. Biochem. Mol. Biol. , vol.39 , pp. 530-553
    • Rezaei-Tavirani, M.1    Moghaddamnia, S.H.2    Ranjbar, B.3    Amani, M.4    Marash, S.A.5
  • 26
    • 58149144559 scopus 로고    scopus 로고
    • Secondary structural change of bovine serum albumin in thermal denaturation up to 130 degrees C and protective effect of sodium dodecyl sulfate on the change
    • Moriyama, Y.; Watanabe, E.; Kobayashi, K.; Harano, H.; Inui, E.; Takeda, K. Secondary structural change of bovine serum albumin in thermal denaturation up to 130 degrees C and protective effect of sodium dodecyl sulfate on the change J. Phys. Chem. B 2008, 51, 16585-16589
    • (2008) J. Phys. Chem. B , vol.51 , pp. 16585-16589
    • Moriyama, Y.1    Watanabe, E.2    Kobayashi, K.3    Harano, H.4    Inui, E.5    Takeda, K.6
  • 27
    • 0017225714 scopus 로고
    • Thermodynamic investigations of proteins. III. Thermodynamic description of lysozyme
    • Pfeil, W.; Privalov, P. L. Thermodynamic investigations of proteins. III. Thermodynamic description of lysozyme Biophys. Chem. 1976, 4, 33-40
    • (1976) Biophys. Chem. , vol.4 , pp. 33-40
    • Pfeil, W.1    Privalov, P.L.2
  • 29
    • 0034513037 scopus 로고    scopus 로고
    • Effect of pro-tonation and PAMAM dendrimer size on the complexation and dynamic mobility of 2-naphthol
    • Kleinman, M. H.; Flory, J. H.; Tomalia, D. A.; Turro, N. J. Effect of pro-tonation and PAMAM dendrimer size on the complexation and dynamic mobility of 2-naphthol J. Phys. Chem. B 2000, 104, 11472-11479
    • (2000) J. Phys. Chem. B , vol.104 , pp. 11472-11479
    • Kleinman, M.H.1    Flory, J.H.2    Tomalia, D.A.3    Turro, N.J.4
  • 30
    • 0027249523 scopus 로고
    • The binding interaction of Coomassie blue with proteins
    • Abert, W. C.; Gregory, W. M.; Allan, G. S. The binding interaction of Coomassie blue with proteins Anal. Biochem. 1993, 213, 407-413
    • (1993) Anal. Biochem. , vol.213 , pp. 407-413
    • Abert, W.C.1    Gregory, W.M.2    Allan, G.S.3
  • 31
    • 35548985771 scopus 로고    scopus 로고
    • Analysis of binding interaction between puerarin and bovine serum albumin by multi-spectroscopic method
    • Xiao, J. B.; Shi, J.; Cao, H.; Wu, S. D.; Ren, F. L.; Xu, M. Analysis of binding interaction between puerarin and bovine serum albumin by multi-spectroscopic method J. Pharm. Biomed. Anal. 2007, 45, 609-615
    • (2007) J. Pharm. Biomed. Anal. , vol.45 , pp. 609-615
    • Xiao, J.B.1    Shi, J.2    Cao, H.3    Wu, S.D.4    Ren, F.L.5    Xu, M.6
  • 32
    • 79960760946 scopus 로고    scopus 로고
    • Analysis of poly(amidoamine) (PAMAM) dendrimer structure by UV-vis spectroscopy
    • Pande, S.; Crooks, R. M. Analysis of poly(amidoamine) (PAMAM) dendrimer structure by UV-vis spectroscopy Langmuir 2011, 27, 9609-9613
    • (2011) Langmuir , vol.27 , pp. 9609-9613
    • Pande, S.1    Crooks, R.M.2
  • 34
    • 41949122581 scopus 로고    scopus 로고
    • GM1-induced structural changes of bovine serum albumin
    • Gayen, A.; Chatterjee, C.; Mukhopadhyay, C. GM1-induced structural changes of bovine serum albumin Biomacromolecules 2008, 9, 974-983
    • (2008) Biomacromolecules , vol.9 , pp. 974-983
    • Gayen, A.1    Chatterjee, C.2    Mukhopadhyay, C.3
  • 35
    • 84901040663 scopus 로고    scopus 로고
    • http://www.dendritech.com/index.html.
  • 36
    • 0016640388 scopus 로고
    • Hydrodynamic structure of bovine serum albumin determined by transient electric birefringence
    • Wright, A. K.; Thompson, M. R. Hydrodynamic structure of bovine serum albumin determined by transient electric birefringence Biophys. J. 1975, 15, 137-141
    • (1975) Biophys. J. , vol.15 , pp. 137-141
    • Wright, A.K.1    Thompson, M.R.2
  • 37
    • 0036148318 scopus 로고    scopus 로고
    • Fluorescence studies on PAMAM dendrimers interactions with bovine serum albumin
    • Klajnert, B.; Bryszewska, M. Fluorescence studies on PAMAM dendrimers interactions with bovine serum albumin Bioelectrochemistry 2002, 55, 33-35
    • (2002) Bioelectrochemistry , vol.55 , pp. 33-35
    • Klajnert, B.1    Bryszewska, M.2
  • 38
    • 3242709482 scopus 로고    scopus 로고
    • Investigation of the interaction between flavonoids and human serum albumin
    • Bi, S. Y.; Ding, L.; Tian, Y.; Song, D. Q.; Zhou, X.; Liu, X.; Zhang, H. Q. Investigation of the interaction between flavonoids and human serum albumin J. Mol. Struct. 2004, 703, 37-45
    • (2004) J. Mol. Struct. , vol.703 , pp. 37-45
    • Bi, S.Y.1    Ding, L.2    Tian, Y.3    Song, D.Q.4    Zhou, X.5    Liu, X.6    Zhang, H.Q.7
  • 39
    • 76249105826 scopus 로고    scopus 로고
    • Complexes of dendrimers with bovine serum albumin
    • Mandeville, J. S.; Tajmir-Riahi, H. A. Complexes of dendrimers with bovine serum albumin Biomacromolecles 2010, 11, 465-472
    • (2010) Biomacromolecles , vol.11 , pp. 465-472
    • Mandeville, J.S.1    Tajmir-Riahi, H.A.2
  • 40
    • 0015936843 scopus 로고
    • Physicochemical aspects of drug-protein interactions: A general perspective
    • Klotz, I. M. Physicochemical aspects of drug-protein interactions: a general perspective Ann. N.Y. Acad. Sci. 1973, 226, 18-25
    • (1973) Ann. N.Y. Acad. Sci. , vol.226 , pp. 18-25
    • Klotz, I.M.1
  • 41
    • 0019889063 scopus 로고
    • Thermodynamics of protein association reactions: Forces contributing to stability
    • Ross, P. D.; Subramanian, S. Thermodynamics of protein association reactions: forces contributing to stability Biochemistry 1981, 20, 3096-3102
    • (1981) Biochemistry , vol.20 , pp. 3096-3102
    • Ross, P.D.1    Subramanian, S.2
  • 42
    • 84888371423 scopus 로고    scopus 로고
    • Comparative Studies of the Binding of Six Phthalate Plasticizers to Pepsin by Multispectroscopic Approach and Molecular Modeling
    • Wang, Y. Q.; Zhang, H. M. Comparative Studies of the Binding of Six Phthalate Plasticizers to Pepsin by Multispectroscopic Approach and Molecular Modeling J. Agric. Food. Chem. 2013, 61, 11191-11200
    • (2013) J. Agric. Food. Chem. , vol.61 , pp. 11191-11200
    • Wang, Y.Q.1    Zhang, H.M.2


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