Registro:

Referencias:

• Hartmann, M., Ordered Mesoporous Materials for Bioadsorption and Biocatalysis (2005) Chem. Mater., 17, pp. 4577-4593
• Bhakta, S.A., Evans, E., Benavidez, T.E., Garcia, C.D., Protein Adsorption onto Nanomaterials for the Development of Biosensors and Analytical Devices: A Review (2015) Anal. Chim. Acta, 872, pp. 7-25
• Bellino, M.G., Regazzoni, A.E., Soler-Illia, G.J.A.A., Amylase-Functionalized Mesoporous Silica Thin Films as Robust Biocatalyst Platforms (2010) ACS Appl. Mater. Interfaces, 2, pp. 360-365
• Rabe, M., Verdes, D., Seeger, S., Understanding Protein Adsorption Phenomena at Solid Surfaces (2011) Adv. Colloid Interface Sci., 162, pp. 87-106
• Gray, J.J., The Interaction of Proteins with Solid Surfaces (2004) Curr. Opin. Struct. Biol., 14, pp. 110-115
• Wei, T., Carignano, M.A., Szleifer, I., Molecular Dynamics Simulation of Lysozyme Adsorption/Desorption on Hydrophobic Surfaces (2012) J. Phys. Chem. B, 116, pp. 10189-10194
• Van Der Veen, M., Norde, W., Stuart, M.C., Electrostatic Interactions in Protein Adsorption Probed by Comparing Lysozyme and Succinylated Lysozyme (2004) Colloids Surf., B, 35, pp. 33-40
• Meissner, J., Prause, A., Bharti, B., Findenegg, G.H., Characterization of Protein Adsorption onto Silica Nanoparticles: Influence of PH and Ionic Strength (2015) Colloid Polym. Sci., 293, pp. 3381-3391
• Wittemann, A., Ballauff, M., Interaction of Proteins with Linear Polyelectrolytes and Spherical Polyelectrolyte Brushes in Aqueous Solution (2006) Phys. Chem. Chem. Phys., 8, pp. 5269-5275
• Bremer, M.G., Duval, J., Norde, W., Lyklema, J., Electrostatic Interactions between Immunoglobulin (IgG) Molecules and a Charged Sorbent (2004) Colloids Surf., A, 250, pp. 29-42
• Chen, K., Xu, Y., Rana, S., Miranda, O.R., Dubin, P.L., Rotello, V.M., Sun, L., Guo, X., Electrostatic Selectivity in Protein-Nanoparticle Interactions (2011) Biomacromolecules, 12, pp. 2552-2561
• Levin, A., Czeslik, C., Interaction of Calmodulin with Poly(Acrylic Acid) Brushes: Effects of High Pressure, PH-Value and Ligand Binding (2018) Colloids Surf., B, 171, pp. 478-484
• Demanèche, S., Chapel, J.-P., Monrozier, L.J., Quiquampoix, H., Dissimilar PH-Dependent Adsorption Features of Bovine Serum Albumin and α-Chymotrypsin on Mica Probed by AFM (2009) Colloids Surf., B, 70, pp. 226-231
• Höök, F., Rodahl, M., Kasemo, B., Brzezinski, P., Structural Changes in Hemoglobin during Adsorption to Solid Surfaces: Effects of PH, Ionic Strength, and Ligand Binding (1998) Proc. Natl. Acad. Sci. U.S.A., 95, pp. 12271-12276
• Rosenfeldt, S., Wittemann, A., Ballauff, M., Breininger, E., Bolze, J., Dingenouts, N., Interaction of Proteins with Spherical Polyelectrolyte Brushes in Solution as Studied by Small-Angle x-Ray Scattering (2004) Phys. Rev. e, 70, p. 061403
• Henzler, K., Haupt, B., Lauterbach, K., Wittemann, A., Borisov, O., Ballauff, M., Adsorption of β-Lactoglobulin on Spherical Polyelectrolyte Brushes: Direct Proof of Counterion Release by Isothermal Titration Calorimetry (2010) J. Am. Chem. Soc., 132, pp. 3159-3163
• Galisteo, F., Norde, W., Adsorption of Lysozyme and α-Lactalbumin on Poly(Styrenesulphonate) Latices 1. Adsorption and Desorption Behaviour (1995) Colloids Surf., B, 4, pp. 375-387
• Biesheuvel, P.M., Van Der Veen, M., Norde, W., A Modified Poisson- Boltzmann Model Including Charge Regulation for the Adsorption of Ionizable Polyelectrolytes to Charged Interfaces, Applied to Lysozyme Adsorption on Silica (2005) J. Phys. Chem. B, 109, pp. 4172-4180
• Longo, G.S., Szleifer, I., Adsorption and Protonation of Peptides and Proteins in PH Responsive Gels (2016) J. Phys.: Appl. Phys., 49, p. 323001
• Lund, M., Åkesson, T., Jönsson, B., Enhanced Protein Adsorption Due to Charge Regulation (2005) Langmuir, 21, pp. 8385-8388
• Yigit, C., Kanduč, M., Ballauff, M., Dzubiella, J., Interaction of Charged Patchy Protein Models with Like-Charged Polyelectrolyte Brushes (2017) Langmuir, 33, pp. 417-427
• Peng, C., Liu, J., Zhao, D., Zhou, J., Adsorption of Hydrophobin on Different Self-Assembled Monolayers: The Role of the Hydrophobic Dipole and the Electric Dipole (2014) Langmuir, 30, pp. 11401-11411
• Ninham, B.W., Parsegian, A., Electrostatic Potential between Surfaces Bearing Ionizable Groups in Ionic Equilibrium with Physiological Saline Solution (1971) J. Theor. Biol., 31, p. 405
• Nap, R., Gong, P., Szleifer, I., Weak Polyelectrolytes Tethered to Surfaces: Effect of Geometry, Acid-Base Equilibrium and Electrical Permittivity (2006) J. Polym. Sci., Part B: Polym. Phys., 44, pp. 2638-2662
• Tagliazucchi, M., Calvo, E.J., Szleifer, I., Molecular Theory of Chemically Modified Electrodes by Redox Polyelectrolytes under Equilibrium Conditions: Comparison with Experiment (2008) J. Phys. Chem. C, 112, pp. 458-471
• Ricci, A.M., Tagliazucchi, M., Calvo, E.J., Charge Regulation in Redox Active Monolayers Embedded in Proton Exchanger Surfaces (2012) Phys. Chem. Chem. Phys., 14, p. 9988
• Tagliazucchi, M., Azzaroni, O., Szleifer, I., Responsive Polymers End-Tethered in Solid-State Nanochannels: When Nanoconfinement Really Matters (2010) J. Am. Chem. Soc., 132, pp. 12404-12411
• Stanton, C.L., Houk, K.N., Benchmarking pKa Prediction Methods for Residues in Proteins (2008) J. Chem. Theory Comput., 4, pp. 951-966
• Bashford, D., Karplus, M., Multiple-Site Titration Curves of Proteins: An Analysis of Exact and Approximate Methods for Their Calculation (1991) J. Phys. Chem., 95, pp. 9556-9561
• Tagliazucchi, M., Szleifer, I., Stimuli-Responsive Polymers Grafted to Nanopores and Other Nano-Curved Surfaces: Structure, Chemical Equilibrium and Transport (2012) Soft Matter, 8, p. 7292
• Kubiak-Ossowska, K., Jachimska, B., Mulheran, P.A., How Negatively Charged Proteins Adsorb to Negatively Charged Surfaces: A Molecular Dynamics Study of BSA Adsorption on Silica (2016) J. Phys. Chem. B, 120, pp. 10463-10468
• Hladílková, J., Callisen, T.H., Lund, M., Lateral Protein-Protein Interactions at Hydrophobic and Charged Surfaces as a Function of PH and Salt Concentration (2016) J. Phys. Chem. B, 120, pp. 3303-3310
• Swails, J.M., Roitberg, A.E., Enhancing Conformation and Protonation State Sampling of Hen Egg White Lysozyme Using PH Replica Exchange Molecular Dynamics (2012) J. Chem. Theory Comput., 8, pp. 4393-4404
• Li, L., Li, C., Sarkar, S., Zhang, J., Witham, S., Zhang, Z., Wang, L., Alexov, E., DelPhi: A Comprehensive Suite for DelPhi Software and Associated Resources (2012) BMC Biophys., 5, p. 9
• Vorobjev, Y.N., Vila, J.A., Scheraga, H.A., FAMBE-PH: A Fast and Accurate Method to Compute the Total Solvation Free Energies of Proteins (2008) J. Phys. Chem. B, 112, pp. 11122-11136
• Alexov, E.G., Gunner, M.R., Incorporating Protein Conformational Flexibility into the Calculation of PH-Dependent Protein Properties (1997) Biophys. J., 72, pp. 2075-2093
• Li, H., Robertson, A.D., Jensen, J.H., Very Fast Empirical Prediction and Rationalization of Protein PKa Values (2005) Proteins, 61, pp. 704-721
• De Vos, W.M., Leermakers, F.A.M., De Keizer, A., Stuart, M.A.C., Kleijn, J.M., Field Theoretical Analysis of Driving Forces for the Uptake of Proteins by Like-Charged Polyelectrolyte Brushes: Effects of Charge Regulation and Patchiness (2010) Langmuir, 26, pp. 249-259
• Fogolari, F., Briggs, J.M., On the Variational Approach to Poisson-Boltzmann Free Energies (1997) Chem. Phys. Lett., 281, pp. 135-139
• Berisio, R., Sica, F., Lamzin, V., Wilson, K., Zagari, A., Mazzarella, L., Atomic Resolution Structures of Ribonuclease A at Six PH Values (2002) Acta Crystallogr., Sect. D: Biol. Crystallogr., 58, pp. 441-450
• Ramasubbu, N., Paloth, V., Luo, Y., Brayer, G., Levine, M., Structure of Human Salivary A-amylase at 1.6 Å Resolution: Implications for Its Role in the Oral Cavity (1996) Acta Crystallogr., Sect. D: Biol. Crystallogr., 52, pp. 435-446
• Kontopidis, G., Gilliver, A.N., Sawyer, L., Ovine B-lactoglobulin at Atomic Resolution (2014) Acta Crystallogr., Sect. F: Struct. Biol. Commun., 70, pp. 1498-1503
• Basch, J.J., Timasheff, S.N., Hydrogen Ion Equilibria of the Genetic Variants of Bovine β-Lactoglobulin (1967) Arch. Biochem. Biophys., 118, pp. 37-47
• Taulier, N., Chalikian, T.V., Characterization of PH-Induced Transitions of β-Lactoglobulin: Ultrasonic, Densimetric, and Spectroscopic Studies (2001) J. Mol. Biol., 314, pp. 873-889
• Haynes, C.A., Sliwinsky, E., Norde, W., Structural and Electrostatic Properties of Globular Proteins at a Polystyrene-Water Interface (1994) J. Colloid Interface Sci., 164, pp. 394-409
• Tanford, C., Hauenstein, J.D., Hydrogen Ion Equilibria of Ribonuclease1 (1956) J. Am. Chem. Soc., 78, pp. 5287-5291
• Webb, H., Tynan-Connolly, B.M., Lee, G.M., Farrell, D., O'Meara, F., Søndergaard, C.R., Teilum, K., Nielsen, J.E., Remeasuring HEWL PKa Values by NMR Spectroscopy: Methods, Analysis, Accuracy, and Implications for Theoretical PKa Calculations (2011) Proteins: Struct., Funct., Genet., 79, pp. 685-702
• Lee, S.J., Park, K., Protein Interaction with Surfaces: Separation Distance-dependent Interaction Energies (1994) J. Vac. Sci. Technol., A, 12, pp. 2949-2955
• Kubiak-Ossowska, K., Cwieka, M., Kaczynska, A., Jachimska, B., Mulheran, P.A., Lysozyme Adsorption at a Silica Surface Using Simulation and Experiment: Effects of PH on Protein Layer Structure (2015) Phys. Chem. Chem. Phys., 17, pp. 24070-24077
• Kubiak-Ossowska, K., Mulheran, P.A., Mechanism of Hen Egg White Lysozyme Adsorption on a Charged Solid Surface (2010) Langmuir, 26, pp. 15954-15965
• Hildebrand, N., Köppen, S., Derr, L., Li, K., Koleini, M., Rezwan, K., Ciacchi, L.C., Adsorption Orientation and Binding Motifs of Lysozyme and Chymotrypsin on Amorphous Silica (2015) J. Phys. Chem. C, 119, pp. 7295-7307
• Yu, G., Liu, J., Zhou, J., Mesoscopic Coarse-Grained Simulations of Lysozyme Adsorption (2014) J. Phys. Chem. B, 118, pp. 4451-4460
• Ellis, C.R., Shen, J., PH-Dependent Population Shift Regulates BACE1 Activity and Inhibition (2015) J. Am. Chem. Soc., 137, pp. 9543-9546
• Clement, G.E., Snyder, S.L., Price, H., Cartmell, R., The PH Dependence of the Pepsin-Catalyzed Hydrolysis of Neutral Dipeptides (1968) J. Am. Chem. Soc., 90, pp. 5603-5610
• Loewen, P.C., Carpena, X., Vidossich, P., Fita, I., Rovira, C., An Ionizable Active-Site Tryptophan Imparts Catalase Activity to a Peroxidase Core (2014) J. Am. Chem. Soc., 136, pp. 7249-7252
• Gascón, V., Márquez-Álvarez, C., Blanco, R.M., Efficient Retention of Laccase by Non-Covalent Immobilization on Amino-Functionalized Ordered Mesoporous Silica (2004) Appl. Catal., A, 482, pp. 116-126
• Frančič, N., Bellino, M.G., Soler-Illia, G.J., Lobnik, A., Mesoporous Titania Thin Films as Efficient Enzyme Carriers for Paraoxon Determination/Detoxification: Effects of Enzyme Binding and Pore Hierarchy on the Biocatalyst Activity and Reusability (2014) Analyst, 139, pp. 3127-3136

Citas:

---------- APA ----------

---------- CHICAGO ----------

---------- MLA ----------

---------- VANCOUVER ----------