메뉴 건너뛰기




Volumn 9, Issue 2, 2013, Pages 5070-5079

Human insulin adsorption kinetics, conformational changes and amyloidal aggregate formation on hydrophobic surfaces

Author keywords

Fourier transform infrared spectroscopy (FTIR); Insulin; Protein adsorption on material surfaces; Protein aggregation; Surface plasmon resonance imaging (SPRi)

Indexed keywords

ADSORPTION; AGGREGATES; AMIDES; FOURIER TRANSFORM INFRARED SPECTROSCOPY; HYDROPHOBICITY; INSULIN; MEDICAL IMAGING; PROTEINS; SURFACE CHEMISTRY; SURFACE PLASMON RESONANCE;

EID: 84872095196     PISSN: 17427061     EISSN: 18787568     Source Type: Journal    
DOI: 10.1016/j.actbio.2012.09.025     Document Type: Article
Times cited : (39)

References (34)
  • 2
    • 0001419932 scopus 로고
    • The X-ray interpretation of denaturation and the structure of the seed globulins
    • W.T. Astbury, S. Dickinson, and K. Bailey The X-ray interpretation of denaturation and the structure of the seed globulins Biochem J 29 1935 2351 2360.1
    • (1935) Biochem J , vol.29 , pp. 2351-23601
    • Astbury, W.T.1    Dickinson, S.2    Bailey, K.3
  • 3
    • 0033200063 scopus 로고    scopus 로고
    • Protein misfolding, evolution and disease
    • C.M. Dobson Protein misfolding, evolution and disease Trends Biochem Sci 24 1999 329 332
    • (1999) Trends Biochem Sci , vol.24 , pp. 329-332
    • Dobson, C.M.1
  • 4
    • 0037818986 scopus 로고
    • The proteins of the mammalian epidermis
    • K.M. Rudall The proteins of the mammalian epidermis Adv Protein Chem 7 1952 253 290
    • (1952) Adv Protein Chem , vol.7 , pp. 253-290
    • Rudall, K.M.1
  • 5
    • 0033621165 scopus 로고    scopus 로고
    • Amyloid diseases: Abnormal protein aggregation in neurodegeneration
    • E.H. Koo, P.T. Lansbury, and J.W. Kelly Amyloid diseases: abnormal protein aggregation in neurodegeneration Proc Natl Acad Sci USA 96 1999 9989 9990
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 9989-9990
    • Koo, E.H.1    Lansbury, P.T.2    Kelly, J.W.3
  • 7
    • 0021134512 scopus 로고
    • Effect of contact material on vibration-induced insulin aggregation
    • V. Feingold, A.B. Jenkins, and E.W. Kraegen Effect of contact material on vibration-induced insulin aggregation Diabetologia 27 1984 373 378
    • (1984) Diabetologia , vol.27 , pp. 373-378
    • Feingold, V.1    Jenkins, A.B.2    Kraegen, E.W.3
  • 9
    • 0021166019 scopus 로고
    • Adsorption isotherms of insulin onto various materials
    • M.V. Sefton, and G.M. Antonacci Adsorption isotherms of insulin onto various materials Diabetes 33 1984 674 680
    • (1984) Diabetes , vol.33 , pp. 674-680
    • Sefton, M.V.1    Antonacci, G.M.2
  • 11
  • 14
    • 0033616587 scopus 로고    scopus 로고
    • In situ atomic force microscopy study of Alzheimer's beta-Amyloid peptide on different substrates: New insights into mechanism of beta-sheet formation
    • T. Kowalewski, and D.M. Holtzman In situ atomic force microscopy study of Alzheimer's beta-Amyloid peptide on different substrates: new insights into mechanism of beta-sheet formation Proc Natl Acad Sci USA 96 1999 3688 3693
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 3688-3693
    • Kowalewski, T.1    Holtzman, D.M.2
  • 15
    • 0345688752 scopus 로고    scopus 로고
    • Influence of hydrophobic Teflon particles on the structure of amyloid beta-peptide
    • C.E. Giacomelli, and W. Norde Influence of hydrophobic Teflon particles on the structure of amyloid beta-peptide Biomacromolecules 4 2003 1719 1726
    • (2003) Biomacromolecules , vol.4 , pp. 1719-1726
    • Giacomelli, C.E.1    Norde, W.2
  • 16
    • 18844378631 scopus 로고    scopus 로고
    • Surface-induced aggregation of beta amyloid peptide by ω-substituted alkanethiol monolayers supported on gold
    • M.J. McMasters, R.P. Hammer, and R.L. McCarley Surface-induced aggregation of beta amyloid peptide by ω-substituted alkanethiol monolayers supported on gold Langmuir 21 2005 4464 4470
    • (2005) Langmuir , vol.21 , pp. 4464-4470
    • McMasters, M.J.1    Hammer, R.P.2    McCarley, R.L.3
  • 17
    • 77952775252 scopus 로고    scopus 로고
    • Amyloid-beta fibrillogenesis seeded by interface-induced peptide misfolding and self-Assembly
    • E.Y. Chi, S.L. Frey, A. Winans, K.L.H. Lam, K. Kjaer, and J. Majewski Amyloid-beta fibrillogenesis seeded by interface-induced peptide misfolding and self-Assembly Biophys J 98 2010 2299 2308
    • (2010) Biophys J , vol.98 , pp. 2299-2308
    • Chi, E.Y.1    Frey, S.L.2    Winans, A.3    Lam, K.L.H.4    Kjaer, K.5    Majewski, J.6
  • 18
    • 0032796425 scopus 로고    scopus 로고
    • Amyloid-beta-sheet formation at the air-water interface
    • C. Schladitz, E.P. Vieira, H. Hermel, and H. Möhwald Amyloid-beta-sheet formation at the air-water interface Biophys J 77 1999 3305 3310
    • (1999) Biophys J , vol.77 , pp. 3305-3310
    • Schladitz, C.1    Vieira, E.P.2    Hermel, H.3    Möhwald, H.4
  • 19
    • 0026004620 scopus 로고
    • Kinetics of insulin aggregation in aqueous solutions upon agitation in the presence of hydrophobic surfaces
    • V. Sluzky, J. Tamada, A. Klibanov, and R. Langer Kinetics of insulin aggregation in aqueous solutions upon agitation in the presence of hydrophobic surfaces Proc Natl Acad Sci USA 88 1991 9377 9381
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 9377-9381
    • Sluzky, V.1    Tamada, J.2    Klibanov, A.3    Langer, R.4
  • 20
    • 0026698922 scopus 로고
    • Mechanism of insulin aggregation and stabilization in agitated aqueous solutions
    • V. Sluzky, A.M. Klibanov, and R. Langer Mechanism of insulin aggregation and stabilization in agitated aqueous solutions Biotechnol Bioeng 40 1992 895 903
    • (1992) Biotechnol Bioeng , vol.40 , pp. 895-903
    • Sluzky, V.1    Klibanov, A.M.2    Langer, R.3
  • 22
    • 0037150332 scopus 로고    scopus 로고
    • Comparison of the structure of polyelectrolyte multilayer films exhibiting a linear and an exponential growth regime: An in situ atomic force microscopy study
    • P. Lavalle, C. Gergely, F.J.G. Cuisinier, G. Decher, P. Schaaf, and J.C. Voegel Comparison of the structure of polyelectrolyte multilayer films exhibiting a linear and an exponential growth regime: an in situ atomic force microscopy study Macromolecules 35 2002 4458 4465
    • (2002) Macromolecules , vol.35 , pp. 4458-4465
    • Lavalle, P.1    Gergely, C.2    Cuisinier, F.J.G.3    Decher, G.4    Schaaf, P.5    Voegel, J.C.6
  • 23
    • 0035827748 scopus 로고    scopus 로고
    • Determination of structural parameters characterizing thin films by optical methods: A comparison between scanning angle reflectometry and optical waveguide lightmode spectroscopy
    • C. Picart, G. Ladam, B. Senger, J.-C. Voegel, P. Schaaf, and F.J.G. Cuisinier Determination of structural parameters characterizing thin films by optical methods: a comparison between scanning angle reflectometry and optical waveguide lightmode spectroscopy J Chem Phys 115 2001 1086
    • (2001) J Chem Phys , vol.115 , pp. 1086
    • Picart, C.1    Ladam, G.2    Senger, B.3    Voegel, J.-C.4    Schaaf, P.5    Cuisinier, F.J.G.6
  • 25
    • 0036880493 scopus 로고    scopus 로고
    • What vibrations tell us about proteins
    • A. Barth, and C. Zscherp What vibrations tell us about proteins Q Rev Biophys 35 2002 369 430
    • (2002) Q Rev Biophys , vol.35 , pp. 369-430
    • Barth, A.1    Zscherp, C.2
  • 26
    • 3042665537 scopus 로고    scopus 로고
    • Insulin forms amyloid in a strain-dependent manner: An FT-IR spectroscopic study
    • W. Dzwolak, V. Smirnovas, R. Jansen, and R. Winter Insulin forms amyloid in a strain-dependent manner: an FT-IR spectroscopic study Protein Sci 13 2004 1927 1932
    • (2004) Protein Sci , vol.13 , pp. 1927-1932
    • Dzwolak, W.1    Smirnovas, V.2    Jansen, R.3    Winter, R.4
  • 27
    • 0033777523 scopus 로고    scopus 로고
    • Formation of insulin amyloid fibrils followed by FTIR simultaneously with CD and electron microscopy
    • M. Bouchard, J. Zurdo, E. Nettleton, C.M. Dobson, and C.V. Robinson Formation of insulin amyloid fibrils followed by FTIR simultaneously with CD and electron microscopy Protein 9 2000 1960 1967
    • (2000) Protein , vol.9 , pp. 1960-1967
    • Bouchard, M.1    Zurdo, J.2    Nettleton, E.3    Dobson, C.M.4    Robinson, C.V.5
  • 28
    • 9344243513 scopus 로고    scopus 로고
    • FTIR reveals structural differences between native beta-sheet proteins and amyloid fibrils
    • G. Zandomeneghi, M.R.H. Krebs, M.G. McCammon, and M. Fändrich FTIR reveals structural differences between native beta-sheet proteins and amyloid fibrils Protein Sci 13 2004 3314 3321
    • (2004) Protein Sci , vol.13 , pp. 3314-3321
    • Zandomeneghi, G.1    Krebs, M.R.H.2    McCammon, M.G.3    Fändrich, M.4
  • 29
    • 34548094323 scopus 로고    scopus 로고
    • Fourier transform infrared spectroscopic analysis of protein secondary structures
    • J. Kong, and S. Yu Fourier transform infrared spectroscopic analysis of protein secondary structures Acta Biochim Biophys Sin 39 2007 549 559
    • (2007) Acta Biochim Biophys Sin , vol.39 , pp. 549-559
    • Kong, J.1    Yu, S.2
  • 30
    • 0010761936 scopus 로고
    • Spectroscopic investigation of the strength of hydrogen bonds formed by amides
    • S.-I. Mizushima, M. Tsuboi, T. Shimanouchi, and Y. Tsuda Spectroscopic investigation of the strength of hydrogen bonds formed by amides Spectrochim Acta 7 1955 100 107
    • (1955) Spectrochim Acta , vol.7 , pp. 100-107
    • Mizushima, S.-I.1    Tsuboi, M.2    Shimanouchi, T.3    Tsuda, Y.4
  • 31
    • 33748348632 scopus 로고    scopus 로고
    • Redox infrared markers of the heme and axial ligands in microperoxidase: Bases for the analysis of c-type cytochromes
    • L. Marboutin, A. Boussac, and C. Berthomieu Redox infrared markers of the heme and axial ligands in microperoxidase: bases for the analysis of c-type cytochromes J Biol Inorg Chem 11 2006 811 823
    • (2006) J Biol Inorg Chem , vol.11 , pp. 811-823
    • Marboutin, L.1    Boussac, A.2    Berthomieu, C.3
  • 32
    • 33748778466 scopus 로고    scopus 로고
    • Determining beta-sheet crystallinity in fibrous proteins by thermal analysis and infrared spectroscopy
    • X. Hu, D. Kaplan, and P. Cebe Determining beta-sheet crystallinity in fibrous proteins by thermal analysis and infrared spectroscopy Macromolecules 39 2006 6161 6170
    • (2006) Macromolecules , vol.39 , pp. 6161-6170
    • Hu, X.1    Kaplan, D.2    Cebe, P.3
  • 33
    • 61549102154 scopus 로고    scopus 로고
    • Interaction of IAPP and insulin with model interfaces studied using neutron reflectometry
    • C. Jeworrek, O. Hollmann, R. Steitz, R. Winter, and C. Czeslik Interaction of IAPP and insulin with model interfaces studied using neutron reflectometry Biophys J 96 2009 1115 1123
    • (2009) Biophys J , vol.96 , pp. 1115-1123
    • Jeworrek, C.1    Hollmann, O.2    Steitz, R.3    Winter, R.4    Czeslik, C.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.