메뉴 건너뛰기




Volumn 88, Issue 2, 2014, Pages 325-331

Complex coacervates of hyaluronic acid and lysozyme: Effect on protein structure and physical stability

Author keywords

Binding characteristics; Bovine serum albumin; Complex coacervation; Differential scanning calorimetry; Differential scanning fluorimetry; Hyaluronan; Hydrogel; Isothermal titration calorimetry; Sodium hyaluronate; Stability

Indexed keywords

BOVINE SERUM ALBUMIN; HYALURONIC ACID; LYSOZYME; SODIUM CHLORIDE;

EID: 84908368377     PISSN: 09396411     EISSN: 18733441     Source Type: Journal    
DOI: 10.1016/j.ejpb.2014.09.001     Document Type: Article
Times cited : (70)

References (35)
  • 1
    • 84871663410 scopus 로고    scopus 로고
    • Chitosan-hyaluronic acid nanoparticles for gene silencing: The role of hyaluronic acid on the nanoparticles' formation and activity
    • S. Al-Qadi, M. Alatorre-Meda, E.M. Zaghloul, P. Taboada, and C. Remunán-López Chitosan-hyaluronic acid nanoparticles for gene silencing: the role of hyaluronic acid on the nanoparticles' formation and activity Colloids Surf., B: Biointerfaces 103 2013 615 623
    • (2013) Colloids Surf., B: Biointerfaces , vol.103 , pp. 615-623
    • Al-Qadi, S.1    Alatorre-Meda, M.2    Zaghloul, E.M.3    Taboada, P.4    Remunán-López, C.5
  • 3
    • 0014595905 scopus 로고
    • Thermodynamics of the denaturation of lysozyme by guanidine hydrochloride. I. Dependence on pH at 25°∗
    • K. Aune, and C. Tanford Thermodynamics of the denaturation of lysozyme by guanidine hydrochloride. I. Dependence on pH at 25°∗ Biochemistry 1969 4579 4585
    • (1969) Biochemistry , pp. 4579-4585
    • Aune, K.1    Tanford, C.2
  • 4
    • 16644403054 scopus 로고    scopus 로고
    • Viscosupplementation for treatment of osteoarthritis: From initial discovery to current status and results
    • E.A. Balazs Viscosupplementation for treatment of osteoarthritis: from initial discovery to current status and results Surg. Technol. Int. 12 2004 278 289
    • (2004) Surg. Technol. Int. , vol.12 , pp. 278-289
    • Balazs, E.A.1
  • 5
    • 0025700523 scopus 로고
    • Functional properties of hemoglobin immobilized in coacervates prepared from gelatin A and polyanionic carbohydrates
    • M. Brouwer, R. Cashon, and J. Bonaventura Functional properties of hemoglobin immobilized in coacervates prepared from gelatin A and polyanionic carbohydrates Biotechnol. Bioeng. 35 1990 831 836
    • (1990) Biotechnol. Bioeng. , vol.35 , pp. 831-836
    • Brouwer, M.1    Cashon, R.2    Bonaventura, J.3
  • 6
    • 0000778476 scopus 로고
    • Complex colloid systems
    • H.R. Kruyt, Elsevier Publishing Company New York
    • H.G. Bungenberg de Jong Complex colloid systems H.R. Kruyt, Colloid Science 1949 Elsevier Publishing Company New York 335 432
    • (1949) Colloid Science , pp. 335-432
    • Bungenberg De Jong, H.G.1
  • 7
    • 33846814867 scopus 로고    scopus 로고
    • How does dextran sulfate prevent heat induced aggregation of protein? the mechanism and its limitation as aggregation inhibitor
    • K. Chung, J. Kim, B.-K. Cho, B.-J. Ko, B.-Y. Hwang, and B.-G. Kim How does dextran sulfate prevent heat induced aggregation of protein? The mechanism and its limitation as aggregation inhibitor Biochim. Biophys. Acta 1774 2007 249 257
    • (2007) Biochim. Biophys. Acta , vol.1774 , pp. 249-257
    • Chung, K.1    Kim, J.2    Cho, B.-K.3    Ko, B.-J.4    Hwang, B.-Y.5    Kim, B.-G.6
  • 9
    • 0025357111 scopus 로고
    • Protein secondary structures in water from second-derivative amide i infrared spectra
    • A. Dong, P. Huang, and W.S. Caughey Protein secondary structures in water from second-derivative amide I infrared spectra Biochemistry 29 1990 3303 3308
    • (1990) Biochemistry , vol.29 , pp. 3303-3308
    • Dong, A.1    Huang, P.2    Caughey, W.S.3
  • 10
    • 84896762430 scopus 로고    scopus 로고
    • Protein-selective coacervation with hyaluronic acid
    • X. Du, P.L. Dubin, D.A. Hoagland, and L. Sun Protein-selective coacervation with hyaluronic acid Biomacromolecules 15 2014 726 734
    • (2014) Biomacromolecules , vol.15 , pp. 726-734
    • Du, X.1    Dubin, P.L.2    Hoagland, D.A.3    Sun, L.4
  • 11
    • 70350336856 scopus 로고    scopus 로고
    • Polyplex formation between four-arm poly(ethylene oxide)-b-poly(2-(diethylamino)ethyl methacrylate) and plasmid DNA in gene delivery
    • E. He, C.Y. Yue, F. Simeon, L.H. Zhou, H.P. Too, and K.C. Tam Polyplex formation between four-arm poly(ethylene oxide)-b-poly(2-(diethylamino)ethyl methacrylate) and plasmid DNA in gene delivery J. Biomed. Mater. Res. A 91 2009 708 718
    • (2009) J. Biomed. Mater. Res. A , vol.91 , pp. 708-718
    • He, E.1    Yue, C.Y.2    Simeon, F.3    Zhou, L.H.4    Too, H.P.5    Tam, K.C.6
  • 12
    • 77349117275 scopus 로고    scopus 로고
    • Hybrid hyaluronan hydrogel encapsulating nanogel as a protein nanocarrier: New system for sustained delivery of protein with a chaperone-like function
    • T. Hirakura, K. Yasugi, T. Nemoto, M. Sato, T. Shimoboji, Y. Aso, N. Morimoto, and K. Akiyoshi Hybrid hyaluronan hydrogel encapsulating nanogel as a protein nanocarrier: new system for sustained delivery of protein with a chaperone-like function J. Controlled Release 142 2010 483 489
    • (2010) J. Controlled Release , vol.142 , pp. 483-489
    • Hirakura, T.1    Yasugi, K.2    Nemoto, T.3    Sato, M.4    Shimoboji, T.5    Aso, Y.6    Morimoto, N.7    Akiyoshi, K.8
  • 13
    • 79960212031 scopus 로고    scopus 로고
    • On the temperature dependence of complex formation between chitosan and proteins
    • M.R. Kasimova, A. Velazquez-Campoy, and H.M. Nielsen On the temperature dependence of complex formation between chitosan and proteins Biomacromolecules 12 2011 2534 2543
    • (2011) Biomacromolecules , vol.12 , pp. 2534-2543
    • Kasimova, M.R.1    Velazquez-Campoy, A.2    Nielsen, H.M.3
  • 15
    • 0030059491 scopus 로고    scopus 로고
    • Quantitation of the area of overlap between second-derivative amide i infrared spectra to determine the structural similarity of a protein in different states
    • B.S. Kendrick, A. Dong, S.D. Allison, M.C. Manning, and J.F. Carpenter Quantitation of the area of overlap between second-derivative amide I infrared spectra to determine the structural similarity of a protein in different states J. Pharm. Sci. 85 1996 155 158
    • (1996) J. Pharm. Sci. , vol.85 , pp. 155-158
    • Kendrick, B.S.1    Dong, A.2    Allison, S.D.3    Manning, M.C.4    Carpenter, J.F.5
  • 16
    • 61349123258 scopus 로고    scopus 로고
    • Nucleic acid delivery with chitosan and its derivatives
    • W.-F. Lai, and M.C.-M. Lin Nucleic acid delivery with chitosan and its derivatives J. Controlled Release 134 2009 158 168
    • (2009) J. Controlled Release , vol.134 , pp. 158-168
    • Lai, W.-F.1    Lin, M.C.-M.2
  • 17
    • 0141605182 scopus 로고    scopus 로고
    • Preparation and properties of polyelectrolyte complex sponges composed of hyaluronic acid and chitosan and their biological behaviors
    • S.B. Lee, Y.M. Lee, K.W. Song, and M.H. Park Preparation and properties of polyelectrolyte complex sponges composed of hyaluronic acid and chitosan and their biological behaviors J. Appl. Polym. Sci. 90 2003 925 932
    • (2003) J. Appl. Polym. Sci. , vol.90 , pp. 925-932
    • Lee, S.B.1    Lee, Y.M.2    Song, K.W.3    Park, M.H.4
  • 18
    • 58149359281 scopus 로고    scopus 로고
    • Electrostatic interactions between hyaluronan and proteins at pH 4: How do they modulate hyaluronidase activity
    • H. Lenormand, B. Deschrevel, F. Tranchepain, and J.-C. Vincent Electrostatic interactions between hyaluronan and proteins at pH 4: how do they modulate hyaluronidase activity Biopolymers 89 2008 1088 1103
    • (2008) Biopolymers , vol.89 , pp. 1088-1103
    • Lenormand, H.1    Deschrevel, B.2    Tranchepain, F.3    Vincent, J.-C.4
  • 19
    • 84901983106 scopus 로고    scopus 로고
    • Structurally flexible triethanolamine-core poly(amidoamine) dendrimers as effective nanovectors to deliver RNAi-based therapeutics
    • X. Liu, C. Liu, C.V. Catapano, L. Peng, J. Zhou, and P. Rocchi Structurally flexible triethanolamine-core poly(amidoamine) dendrimers as effective nanovectors to deliver RNAi-based therapeutics Biotechnol. Adv. 2013 1 9
    • (2013) Biotechnol. Adv. , pp. 1-9
    • Liu, X.1    Liu, C.2    Catapano, C.V.3    Peng, L.4    Zhou, J.5    Rocchi, P.6
  • 20
    • 33846950077 scopus 로고    scopus 로고
    • Complex coacervation of silk fibroin and hyaluronic acid
    • O. Malay, O. Bayraktar, and A. Batigün Complex coacervation of silk fibroin and hyaluronic acid Int. J. Biol. Macromol. 40 2007 387 393
    • (2007) Int. J. Biol. Macromol. , vol.40 , pp. 387-393
    • Malay, O.1    Bayraktar, O.2    Batigün, A.3
  • 21
    • 0001413280 scopus 로고
    • The polysaccharide of the vitreous humor
    • K. Meyer, and J. Palmer The polysaccharide of the vitreous humor J. Biol. Chem. 1934 629 634
    • (1934) J. Biol. Chem. , pp. 629-634
    • Meyer, K.1    Palmer, J.2
  • 22
    • 79953877321 scopus 로고    scopus 로고
    • Rodlike complexes of a polyelectrolyte (hyaluronan) and a protein (lysozyme) observed by SANS
    • I. Morfin, E. Buhler, F. Cousin, I. Grillo, and F. Boué Rodlike complexes of a polyelectrolyte (hyaluronan) and a protein (lysozyme) observed by SANS Biomacromolecules 12 2011 859 870
    • (2011) Biomacromolecules , vol.12 , pp. 859-870
    • Morfin, I.1    Buhler, E.2    Cousin, F.3    Grillo, I.4    Boué, F.5
  • 23
    • 70449641609 scopus 로고    scopus 로고
    • Dermatan sulfate as a stabilizer for protein stability in poly(lactide-co-glycolide) depot
    • W. Park, and K. Na Dermatan sulfate as a stabilizer for protein stability in poly(lactide-co-glycolide) depot Biotechnol. Bioprocess Eng. 14 2009 668 674
    • (2009) Biotechnol. Bioprocess Eng. , vol.14 , pp. 668-674
    • Park, W.1    Na, K.2
  • 26
    • 84871648096 scopus 로고    scopus 로고
    • DNA-gelatin complex coacervation, UCST and first-order phase transition of coacervate to anisotropic ion gel in 1-methyl-3-octylimidazolium chloride ionic liquid solutions
    • K. Rawat, V.K. Aswal, and H.B. Bohidar DNA-gelatin complex coacervation, UCST and first-order phase transition of coacervate to anisotropic ion gel in 1-methyl-3-octylimidazolium chloride ionic liquid solutions J. Phys. Chem. B 116 2012 14805 14816
    • (2012) J. Phys. Chem. B , vol.116 , pp. 14805-14816
    • Rawat, K.1    Aswal, V.K.2    Bohidar, H.B.3
  • 27
    • 67049087882 scopus 로고    scopus 로고
    • Spatial structure and composition of polysaccharide-protein complexes from small angle neutron scattering
    • I. Schmidt, F. Cousin, C. Huchon, F. Boué, and M.A.V. Axelos Spatial structure and composition of polysaccharide-protein complexes from small angle neutron scattering Biomacromolecules 10 2009 1346 1357
    • (2009) Biomacromolecules , vol.10 , pp. 1346-1357
    • Schmidt, I.1    Cousin, F.2    Huchon, C.3    Boué, F.4    Axelos, M.A.V.5
  • 28
    • 0033609009 scopus 로고    scopus 로고
    • Hyaluronan forms specific stable tertiary structures in aqueous solution: A 13C NMR study
    • J.E. Scott, and F. Heatley Hyaluronan forms specific stable tertiary structures in aqueous solution: a 13C NMR study Proc. Natl. Acad. Sci. USA 96 1999 4850 4855
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 4850-4855
    • Scott, J.E.1    Heatley, F.2
  • 29
    • 70349168548 scopus 로고    scopus 로고
    • Polyanion hydrophobicity and protein basicity affect protein stability in protein-polyanion complexes
    • E. Sedlák, D. Fedunová, V. Veselá, D. Sedláková, and M. Antalík Polyanion hydrophobicity and protein basicity affect protein stability in protein-polyanion complexes Biomacromolecules 10 2009 2533 2538
    • (2009) Biomacromolecules , vol.10 , pp. 2533-2538
    • Sedlák, E.1    Fedunová, D.2    Veselá, V.3    Sedláková, D.4    Antalík, M.5
  • 31
    • 17644419346 scopus 로고    scopus 로고
    • Complex coacervation of lysozyme and heparin: Complex characterization and protein stability
    • M. Van de Weert, M.B. Andersen, and S. Frokjaer Complex coacervation of lysozyme and heparin: complex characterization and protein stability Pharm. Res. 21 2004 2354 2359
    • (2004) Pharm. Res. , vol.21 , pp. 2354-2359
    • Van De Weert, M.1    Andersen, M.B.2    Frokjaer, S.3
  • 32
    • 0035856814 scopus 로고    scopus 로고
    • Factors affecting protein release from alginate-chitosan coacervate microcapsules during production and gastric/intestinal simulation
    • G.W. Vandenberg, C. Drolet, S.L. Scott, and J. de la Noüe Factors affecting protein release from alginate-chitosan coacervate microcapsules during production and gastric/intestinal simulation J. Controlled Release 77 2001 297 307
    • (2001) J. Controlled Release , vol.77 , pp. 297-307
    • Vandenberg, G.W.1    Drolet, C.2    Scott, S.L.3    De La Noüe, J.4
  • 33
    • 29144479964 scopus 로고    scopus 로고
    • Ligand binding to one-dimensional lattice-like macromolecules: Analysis of the McGhee-von Hippel theory implemented in isothermal titration calorimetry
    • A. Velazquez-Campoy Ligand binding to one-dimensional lattice-like macromolecules: analysis of the McGhee-von Hippel theory implemented in isothermal titration calorimetry Anal. Biochem. 348 2006 94 104
    • (2006) Anal. Biochem. , vol.348 , pp. 94-104
    • Velazquez-Campoy, A.1
  • 35
    • 84870242128 scopus 로고    scopus 로고
    • Properties and analytical applications of the self-assembled complex {peroxidase-chitosan}
    • I.A. Veselova, L.I. Malinina, P.V. Rodionov, and T.N. Shekhovtsova Properties and analytical applications of the self-assembled complex {peroxidase-chitosan} Talanta 102 2012 101 109
    • (2012) Talanta , vol.102 , pp. 101-109
    • Veselova, I.A.1    Malinina, L.I.2    Rodionov, P.V.3    Shekhovtsova, T.N.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.