Tytuł artykułuProtein conformational changes induced by adsorption onto material surfaces: an important issue for biomedical applications of material science
Tytuł czasopismaBulletin of the Polish Academy of Sciences: Technical Sciences
NumerNo 2 June
Wydział PANNauki Techniczne
WydawcaPolish Academy of Sciences
IdentyfikatorISSN 0239-7528, eISSN 2300-1917
ReferencjeKleinman H. (2005), Matrigel: basement membrane matrix with biological activity, Semin. Cancer Biol, 15, 5, 378. ; Sordel T. (2007), Influence of glass and polymer coatings on CHO cell morphology and adhesion, Biomaterials, 28, 8, 1572. ; Vogler E. (1995), Contact activation of the plasma coagulation cascade. II. Protein adsorption to procoagulant surfaces, J. Biomed Mater. Res, 29, 8, 1017. ; Vogler E. (1995), Contact activation of the plasma coagulation cascade. I. Procoagulant surface chemistry and energy, J. Biomed Mater. Res, 29, 8, 1005. ; Griffin J. (1978), Role of surface in surface-dependent activation of Hageman factor (blood coagulation factor XII), Proc. Natl. Acad. Sci. USA, 75, 4, 1998. ; Nilsson B. (2007), The role of complement in biomaterial-induced inflammation, Mol. Immunol, 44, 1-3, 82. ; Chenoweth D. (1987), Complement activation in extracorporeal circuits, Ann. NY Acad. Sci, 516, 306. ; Gaboriaud C. (2007), Assembly of C1 and the MBL- and ficolin-MASP complexes: structural insights, Immunobiology, 212, 4-5, 279. ; Gaboriaud C. (2004), Structure and activation of the C1 complex of complement: unraveling the puzzle, Trends Immunol, 25, 7, 368. ; Garlatti V. (2007), Structural basis for innate immune sensing by M-ficolin and its control by a pH-dependent conformational switch, J. Biol. Chem, 282, 49, 35814. ; Vorup-Jensen T. (2000), Distinct pathways of mannanbinding lectin (MBL)- and C1-complex autoactivation revealed by reconstitution of MBL with recombinant MBL-associated serine protease-2, J. Immunol, 165, 4, 2093. ; Gref R. (2000), ‘Stealth’ coronacore nanoparticles surface modified by polyethylene glycol (PEG): influences of the corona (PEG chain length and surface density) and of the core composition on phagocytic uptake and plasma protein adsorption, Colloids Surf. B Biointerfaces, 18, 3-4, 301. ; Branch D. (2001), Long-term stability of grafted polyethylene glycol surfaces for use with microstamped substrates in neuronal cell culture, Biomaterials, 22, 10, 1035. ; Kidane A. (1999), Complement activation by PEO-grafted glass surfaces, J. Biomed Mater. Res, 48, 5, 640. ; Kidane A. (1999), Surface modification with PEO-containing triblock copolymer for improved biocompatibility: in vitro and ex vivo studies, J. Biomater Sci. Polym. Ed, 10, 10, 1089. ; Moghimi S. (2001), Long-circulating and target-specific nanoparticles: theory to practice, Pharmacol Rev, 53, 2, 283. ; Broz P. (2005), Cell targeting by a generic receptor-targeted polymer nanocontainer platform, J. Control Release, 102, 2, 475. ; Stephan S. (2006), Cell-matrix biology in vascular tissue engineering, J. Anat, 209, 4, 495. ; Kapadia M. (2008), Modified prosthetic vascular conduits, Circulation, 117, 14, 1873. ; Sharma B. (2007), Immunogenicity of therapeutic proteins. Part 2: impact of container closures, Biotechnol. Adv, 25, 3, 318. ; Jones L. (2005), Silicone oil induced aggregation of proteins, J. Pharm. Sci, 94, 4, 918. ; Sun L. (1997), Protein denaturation induced by cyclic silicone, Biomaterials, 18, 24, 1593. ; Oi V. (1984), Correlation between segmental flexibility and effecter function of antibodies, Nature, 307, 5947, 136. ; Dearborn D. (1969), Reversible thermal conformation changes in human serum low-density lipoprotein, Proc. Nat. Acad. Sci. USA, 62, 1, 179. ; Uversky V. (2010), The mysterious unfoldome: structureless, underappreciated, yet vital part of any given proteome, J. Biomed. Biotechnol, 5, 680. ; Norde W. (2008), My voyage of discovery to proteins in flatland and beyond, Colloids Surf. B Biointerfaces, 61, 1, 1. ; Gabizon R. (2008), Using peptides to study the interaction between the p53 tetramerization domain and HIV-1 Tat, Biopolymers, 90, 2, 105. ; Higashijima T. (1983), Conformational change of mastoparan from wasp venom on binding with phospholipid membrane, FEBS Lett, 152, 2, 227. ; Brange J. (1986), Neutral insulin solutions physically stabilized by addition of Zn2+, Diabet. Med, 3, 6, 532. ; Hill C. (1991), X-ray structure of an unusual Ca2+ site and the roles of Zn2+ and Ca2+ in the assembly, stability, and storage of the insulin hexamer, Biochemistry, 30, 4, 917. ; Sluzky V. (1991), Kinetics of insulin aggregation in aqueous solutions upon agitation in the presence of hydrophobic surfaces, Proc. Natl. Acad. Sci. USA, 88, 21, 9377. ; Sluzky V. (1992), Mechanism of insulin aggregation and stabilization in agitated aqueous solutions, Biotechnol. Bioeng, 40, 8, 895. ; Feingold V. (1984), Effect of contact material on vibration-induced insulin aggregation, Diabetologia, 27, 3, 373. ; Dathe M. (1990), Insulin aggregation in solution, Int. J. Pept Protein Res, 36, 4, 344. ; Mollmann S. (2005), Adsorption of human insulin and AspB28 insulin on a PTFE-like surface, J. Colloid Interface Sci, 286, 1, 28. ; Hirsch I. (2005), Insulin analogues, N. Engl. J. Med, 352, 2, 174. ; Wollmer A. (1989), Structural transition in the metal-free hexamer of protein-engineered [B13 Gln]insulin, Biol. Chem. Hoppe Seyler, 370, 9, 1045. ; Bentley G. (1992), Role of B13 Glu in insulin assembly. The hexamer structure of recombinant mutant (B13 Glu→Gln) insulin, J. Mol. Biol, 228, 4, 1163. ; Noh H. (2007), Volumetric interpretation of protein adsorption: competition from mixtures and the Vroman effect, Biomaterials, 28, 3, 405. ; Wojciechowski P. (1991), The Vroman effect in tube geometry: the influence of flow on protein adsorption measurements, J. Biomater Sci. Polym. Ed, 2, 3, 203. ; Brash J. (1988), Mechanism of transient adsorption of fibrinogen from plasma to solid surfaces: role of the contact and fibrinolytic systems, Blood, 71, 4, 932. ; Zhou C. (2004), Human immunoglobulin adsorption investigated by means of quartz crystal microbalance dissipation, atomic force microscopy, surface acoustic wave, and surface plasmon resonance techniques, Langmuir, 20, 14, 5870. ; Steinemann S. (1996), Metal implants and surface reactions, Injury, 27, 16, doi.org/10.1016/0020-1383(96)89027-9 ; Disegi J. (2000), Stainless steel in bone surgery, Injury, 31, 2. ; Billington R. (2006), Ion processes in glass ionomer cements, J. Dent, 34, 8, 544. ; Hench L. (2004), Bioactive glasses for in situ tissue regeneration, J. Biomater Sci. Polym. Ed, 15, 4, 543. ; Gehrke S. (1998), Enhanced loading and activity retention of bioactive proteins in hydrogel delivery systems, J. Control Release, 55, 1, 21. ; Crouzier T. (2009), Layer-by-layer films as a biomimetic reservoir for rhBMP-2 delivery: controlled differentiation of myoblasts to osteoblasts, Small, 5, 5, 598. ; Tie Y. (2003), Protein adsorption: kinetics and history dependence, J. Colloid Interface Sci, 268, 1, 1. ; Vallieres K. (2007), AFM imaging of immobilized fibronectin: does the surface conjugation scheme affect the protein orientation/conformation?, Langmuir, 23, 19, 9745. ; Dupont-Guillain C. (2001), AFM Study of the Interaction of Collagen with Polystyrene and Plasma-Oxidized Polystyrene, Langmuir, 17, 7261. ; Hallett P. (1995), Atomic force microscopy of the myosin molecule, Biophys. J, 68, 4, 1604. ; Ando T. (2001), A high-speed atomic force microscope for studying biological macromolecules, Proc. Natl. Acad. Sci. USA, 98, 22, 12468. ; Kodera N. (2003), High-resolution imaging of myosin motor in action by a high-speed atomic force microscope, Adv. Exp. Med. Biol, 538, 119, doi.org/10.1007/978-1-4419-9029-7_11 ; Taniguchi M. (2003), MgATP-induced conformational changes in a single myosin molecule observed by atomic force microscopy: periodicity of substructures in myosin rods, Scanning, 25, 5, 223. ; Richter R. (2005), Following the formation of supported lipid bilayers on mica: a study combining AFM, QCM-D, and ellipsometry, Biophys. J, 88, 5, 3422. ; Han M. (2003), Nanometer-scale roughness having little effect on the amount or structure of adsorbed protein, Langmui, 19, 9868. ; Denis F. (2002), Protein adsorption on model surfaces with controlled nanotopography and chemistry, Langmuir, 18, 819. ; Hayashi T. (2007), Direct observation of interaction between proteins and blood-compatible polymer surfaces, Biointerphases, 2, 119. ; Gergely C. (2002), Multibead-and-spring model to interpret protein detachment studied by AFM force spectroscopy, Biophys. J, 83, 2, 706. ; Merkel R. (1999), Energy landscapes of receptor-ligand bonds explored with dynamic force spectroscopy, Nature, 397, 6714, 50. ; Dubochet J. (1988), Cryo-electron microscopy of vitrified specimens, Q Rev. Biophys, 21, 2, 129. ; Spahn C. (2009), Exploring conformational modes of macromolecular assemblies by multiparticle cryo-EM, Curr. Opin. Struct. Biol, 19, 5, 623. ; Schuette J. (2009), GTPase activation of elongation factor EF-Tu by the ribosome during decoding, EMBO J, 28, 6, 755. ; Sartori A. (2007), Correlative microscopy: bridging the gap between fluorescence light microscopy and cryoelectron tomography, J. Struct. Biol, 160, 2, 135. ; Zhou Z. (2008), Towards atomic resolution structural determination by single-particle cryo-electron microscopy, Curr. Opin. Struct. Biol, 18, 2, 218. ; Orlova E. (2004), Structure determination of macromolecular assemblies by single-particle analysis of cryo-electron micrographs, Curr. Opin. Struct. Biol, 14, 5, 584. ; Zenhausern F. (1993), Solution structure and direct imaging of fibronectin adsorption to solid surfaces by scanning force microscopy and cryoelectron microscopy, J. Electron. Microsc. (Tokyo), 42, 6, 378. ; Baugh L. (2004), Structural changes of fibronectin adsorbed to model surfaces probed by fluorescence resonance energy transfer, J. Biomed. Mater. Res, A 69, 3, 525. ; Baneyx G. (2001), Coexisting conformations of fibronectin in cell culture imaged using fluorescence resonance energy transfer, Proc. Natl. Acad. Sci. USA, 98, 25, 14464. ; Smith M. (2007), Force-induced unfolding of fibronectin in the extracellular matrix of living cells, PLoS Biol, 5, 10, 268. ; Sukumvanich P. (2004), Cellular localization of activated N-WASP using a conformation-sensitive antibody, Cell Motil Cytoskeleton, 59, 2, 141. ; Gorny M. (2002), Human monoclonal antibodies specific for conformation-sensitive epitopes of V3 neutralize human immunodeficiency virus type 1 primary isolates from various clades, J. Virol, 76, 18, 9035. ; Moretto N. (2007), Conformation-sensitive antibodies against alzheimer amyloid-beta by immunization with a thioredoxinconstrained B-cell epitope peptide, J. Biol. Chem, 282, 15, 11436. ; Ueno H. (2007), Novel conformation-sensitive antibodies specific to three- and four-repeat tau, Biochem. Biophys. Res. Commun, 358, 2, 602. ; Jayasena U. (2001), Identification of structural variations in the carboxyl terminus of Alzheimer's disease-associated beta A4[1-42] amyloid using a monoclonal antibody, Clin Exp Immunol, 124, 2, 297. ; Murray K. (2001), Probing the 121-136 domain of lecithin: cholesterol acyltransferase using antibodies, Arch. Biochem. Biophys, 385, 2, 267. ; Andersson G. (1991), Application of four anti-human interferon-alpha monoclonal antibodies for immunoassay and comparative analysis of natural interferon-alpha mixtures, J. Interferon. Res, 11, 1, 53. ; Darst S. (1988), Adsorption of the protein antigen myoglobin affects the binding of conformation-specific monoclonal antibodies, Biophys. J, 53, 4, 533. ; Shields M. (1991), An appraisal of polystyrene-(ELISA) and nitrocellulose-based (ELIFA) enzyme immunoassay systems using monoclonal antibodies reactive toward antigenically distinct forms of human C-reactive protein, J. Immunol. Methods, 141, 2, 253. ; Hocking D. (1996), A novel role for the integrin-binding III-10 module in fibronectin matrix assembly, J. Cell. Biol, 133, 2, 431. ; Chernousov M. (1991), Role of the I-9 and III-1 modules of fibronectin in formation of an extracellular fibronectin matrix, J. Biol. Chem, 266, 17, 10851. ; Meadows P. (2005), Force microscopy studies of fibronectin adsorption and subsequent cellular adhesion to substrates with well-defined surface chemistries, Langmuir, 21, 9, 4096. ; Rodrigues R. (2001), Conformational regulation of the fibronectin binding and alpha 3beta 1 integrin-mediated adhesive activities of thrombospondin-1, J. Biol. Chem, 276, 30, 27913. ; Iuliano D. (1993), Effect of the conformation and orientation of adsorbed fibronectin on endothelial cell spreading and the strength of adhesion, J. Biomed. Mater. Res, 27, 8, 1103. ; Martino M. (2009), Controlling integrin specificity and stem cell differentiation in 2D and 3D environments through regulation of fibronectin domain stability, Biomaterials, 30, 6, 1089. ; Bierbaum S. (2003), Modification of Ti6AL4V surfaces using collagen I, III, and fibronectin. II. Influence on osteoblast responses, J. Biomed. Mater. Res, A 67, 2, 431. ; Bierbaum S. (2003), Modification of Ti6Al4V surfaces using collagen I, III, and fibronectin, Biochemical and morphological characteristics of the adsorbed matrix, J. Biomed. Mater. Res, A 67, 2, 421. ; Jansen R. (2005), Amyloidogenic self-assembly of insulin aggregates probed by high resolution atomic force microscopy, Biophys. J, 88, 2, 1344. ; Manno M. (2006), Kinetics of insulin aggregation: disentanglement of amyloid fibrillation from large-size cluster formation, Biophys. J, 90, 12, 4585. ; Hovgaard M. (2007), Quartz crystal microbalance studies of multilayer glucagon fibrillation at the solid-liquid interface, Biophys. J, 93, 6, 2162. ; Goldsbury C. (1999), Watching amyloid fibrils grow by time-lapse atomic force microscopy, J. Mol. Biol, 285, 1, 33. ; Cheng S. (1994), The conformation of fibronectin on self-assembled monolayers with different surface composition: An FTIR/ATR study, J. Colloid Interface Sci, 162, 135. ; Nocentini M. (1988), Conformational changes of protein adsorbed on polyurethane studied by FTIR-ATR spectroscopy, Microchimica Acta, 94, 343. ; Sethuraman A. (2005), Protein structural perturbation and aggregation on homogeneous surfaces, Biophys. J, 88, 2, 1322. ; Khurana R. (2005), Mechanism of thioflavin T binding to amyloid fibrils, J. Struct. Biol, 151, 3, 229. ; Krebs M. (2005), The mechanism of amyloid spherulite formation by bovine insulin, Biophys. J, 88, 3, 2013. ; Ericsson U. (2006), Thermofluor-based high-throughput stability optimization of proteins for structural studies, Anal. Biochem, 357, 2, 289. ; Vedadi M. (2006), Chemical screening methods to identify ligands that promote protein stability, protein crystallization, and structure determination, Proc. Natl. Acad. Sci. USA, 103, 43, 15835. ; Ferraz N. (2008), Nanopore size affects complement activation, J. Biomed. Mater. Res, A 87, 3, 575. ; Kannan R. (2006), The antithrombogenic potential of a polyhedral oligomeric silsesquioxane (POSS) nanocomposite, Biomacromolecules, 7, 1, 215. ; Schulte V. (2009), Surface topography induces fibroblast adhesion on intrinsically nonadhesive poly(ethylene glycol) substrates, Biomacromolecules, 10, 10, 2795. ; Woodcock S. (2005), Collagen adsorption and structure on polymer surfaces observed by atomic force microscopy, J. Colloid Interface Sci, 292, 1, 99. ; Luthen F. (2005), The influence of surface roughness of titanium on beta1- and beta3-integrin adhesion and the organization of fibronectin in human osteoblastic cells, Biomaterials, 26, 15, 2423. ; Webster T. (2000), Specific proteins mediate enhanced osteoblast adhesion on nanophase ceramics, J. Biomed. Mater. Res, 51, 3, 475. ; Whaley S. (2000), Selection of peptides with semiconductor binding specificity for directed nanocrystal assembly, Nature, 405, 6787, 665. ; Mao C. (2003), Viral assembly of oriented quantum dot nanowires, Proc. Natl. Acad. Sci. USA, 100, 12, 6946. ; Sanghvi A. (2005), Biomaterials functionalization using a novel peptide that selectively binds to a conducting polymer, Nat. Mater, 4, 6, 496. ; Devlin G. (2006), The component polypeptide chains of bovine insulin nucleate or inhibit aggregation of the parent protein in a conformation-dependent manner, J. Mol. Biol, 360, 2, 497. ; Ivanova M. (2006), A systematic screen of beta(2)-microglobulin and insulin for amyloidlike segments, Proc. Natl. Acad. Sci. USA, 103, 11, 4079. ; Tito P. (2000), Dissecting the hydrogen exchange properties of insulin under amyloid fibril forming conditions: a site-specific investigation by mass spectrometry, J. Mol. Biol, 303, 2, 267. ; Ivanova M. (2009), Molecular basis for insulin fibril assembly, Proc. Natl. Acad. Sci. USA, 106, 45, 18990. ; Gunther S. (2007), Docking without docking: ISEARCH-prediction of interactions using known interfaces, Proteins, 69, 4, 839. ; Comeau S. (2004), ClusPro: an automated docking and discrimination method for the prediction of protein complexes, Bioinformatics, 20, 1, 45. ; Negi S. (2007), InterProSurf: a web server for predicting interacting sites on protein surfaces, Bioinformatics, 23, 24, 3397. ; S. de Vries (2006), Intramolecular surface contacts contain information about protein-protein interface regions, Bioinformatics, 22, 17, 2094. ; Neuvirth H. (2004), ProMate: a structure based prediction program to identify the location of protein-protein binding sites, J. Mol. Biol, 338, 1, 181. ; Burgoyne N. (2006), Predicting protein interaction sites: binding hotspots in protein-protein and protein-ligand interfaces, Bioinformatics, 22, 11, 1335. ; Ritchie D. (2008), Recent progress and future directions in protein-protein docking, Curr. Protein Pept. Sci, 9, 1, 1. ; Han P. (2009), Large-scale prediction of long disordered regions in proteins using random forests, BMC Bioinformatics, 10, 8. ; Su C. (2007), iPDA: integrated protein disorder analyzer, Nucleic Acids Res, 35. ; Galzitskaya O. (2006), FoldUnfold: web server for the prediction of disordered regions in protein chain, Bioinformatics, 22, 23, 2948. ; Su C. (2006), Protein disorder prediction by condensed PSSM considering propensity for order or disorder, BMC Bioinformatics, 7, 319. ; Cheng J. (2005), SCRATCH: a protein structure and structural feature prediction server, Nucleic Acids Res, 33, doi.org/10.1093/nar/gki396 ; Dosztanyi Z. (2005), IUPred: web server for the prediction of intrinsically unstructured regions of proteins based on estimated energy content, Bioinformatics, 21, 16, 3433. ; Yang Z. (2005), RONN: the bio-basis function neural network technique applied to the detection of natively disordered regions in proteins, Bioinformatics, 21, 16, 3369. ; Ferron F. (2006), A practical overview of protein disorder prediction methods, Proteins, 65, 1, 1. ; Trovato A. (2007), The PASTA server for protein aggregation prediction, Protein Eng. Des Sel, 20, 10, 521. ; Fernandez-Escamilla A. (2004), Prediction of sequence-dependent and mutational effects on the aggregation of peptides and proteins, Nat. Biotechnol, 22, 10, 1302. ; Tartaglia G. (2008), The Zyggregator method for predicting protein aggregation propensities, Chem. Soc. Rev, 37, 7, 1395. ; Rousseau F. (2006), Protein aggregation and amyloidosis: confusion of the kinds?, Curr. Opin. Struct. Biol, 16, 1, 118. ; Monsellier E. (2007), The distribution of residues in a polypeptide sequence is a determinant of aggregation optimized by evolution, Biophys. J, 93, 12, 4382. ; Smith G. (2005), The structure of T6 bovine insulin, Acta Crystallogr D Biol. Crystallogr, 61, 11, 1476. ; Smith G. (2001), Phase changes in T(3)R(3)(f) human insulin: temperature or pressure induced?, Acta Crystallogr. D Biol Crystallogr, 57, 8, 1091. ; Smith G. (2000), R6 hexameric insulin complexed with mcresol or resorcinol, Acta Crystallogr. D Biol. Crystallogr, 56, 12, 1541. ; Yao Z. (1999), Structure of an insulin dimer in an orthorhombic crystal: the structure analysis of a human insulin mutant (B9 Ser-¿Glu), Acta Crystallogr. D Biol. Crystallogr, 55, 9, 1524. ; Whittingham J. (2002), Insulin at pH 2: structural analysis of the conditions promoting insulin fibre formation, J. Mol. Biol, 318, 2, 479. ; Olsen H. (1996), Solution structure of an engineered insulin monomer at neutral pH, Biochemistry, 35, 27, 8836. ; Moreland J. (2005), The Molecular Biology Toolkit (MBT): a modular platform for developing molecular visualization applications, BMC Bioinformatics, 6, 21.