1,720,981 research outputs found
Adsorption and protonation of peptides and proteins in pH responsive gels
Full text linkTo describe the non-trivial features of the equilibrium protonation and physical adsorption of peptides/proteins in pH-responsive hydrogels, we summarize our recent theoretical work on the subject. In these systems, molecular confinement in nanometer-sized environments modifies the balance between chemical state, physical interactions and molecular organization, which results in a behavior that is qualitatively different from what is expected from assuming the bulk solution protonation. To enhance adsorption, the pH-dependent deprotonation curves of all amino acids of adsorbed proteins are adequately shifted and deformed, which depends, in a complex fashion, on the specific amino acid. This possibility of modifying different acid-base equilibriums gives the adsorbed protein degrees of freedom to regulate charge and enhance electrostatic attractions under a wide range of experimental conditions. Protein adsorption modifies the microenvironment inside the hydrogel, particularly the gel pH. As a result, the state of protonation of the network is different before and after adsorption. The physicochemical considerations described in this review can be useful in the design of functional materials involving protein adsorption.Fil: Longo, Gabriel Sebastian. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Fisicoquímicas Teóricas y Aplicadas. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Instituto de Investigaciones Fisicoquímicas Teóricas y Aplicadas; ArgentinaFil: Szleifer, Igal. Northwestern University; Estados Unido
Controlling swelling/deswelling of stimuli-responsive hydrogel nanofilms in electric fields
Full text linkThe swelling/deswelling transition of pH-sensitive, electrode-grafted, hydrogel nanofilms when exposed to electric fields is studied by theoretical analysis. In acidic conditions, the response of these films to changes in pH is dominated by network-surface interactions, while intra-network electrostatic repulsions, which are highly modulated by the adsorption of salt ions, determine material response at a higher pH. Film thickness is a non-monotonic function of solution pH and displays a local maximum, a local minimum or both, depending on the salt concentration and the applied voltage. We suggest the use of these materials in the development of biosensors and control of enzyme activity.Fil: Longo, Gabriel Sebastian. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Fisicoquímicas Teóricas y Aplicadas. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Instituto de Investigaciones Fisicoquímicas Teóricas y Aplicadas; ArgentinaFil: Olvera De La Cruz, Monica. Northwestern University; Estados UnidosFil: Szleifer, Igal. Northwestern University; Estados Unido
An example of theoretical approaches in polymer hydrogels: insights into the behavior of pH-responsive nanofilms
No full textDue to their self-regulating behavior, pH-responsive hydrogels are frequently considered in the development of functional biomaterials. A rational approach to designing new biomaterials imposes the need to understate their interaction with protein solutions. On the basis of theoretical work, this chapter describes the adsorption of proteins and peptides to films of cross-linked pH-sensitive polymers. Particular emphasis is placed on the physical chemistry that emerges from the charge regulation properties of hydrogels and proteins. As a result of spatial confinement, the acidic units that compose a polymer network modify their protonation state as well as the composition of the surroundings; the local pH drops inside the hydrogel, increasing protein protonation upon adsorption. Having different amino acid residues that protonate or deprotonate under different conditions supplies proteins with degrees of freedom to modify their net charge and, thus, modulate the electrostatic interactions with a given hydrogel that drive adsorption. Tailoring a polymer network’s chemical composition allows for the separation and localization of specific components from multiprotein solutions using pH.Fil: Longo, Gabriel Sebastian. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Fisicoquímicas Teóricas y Aplicadas. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Instituto de Investigaciones Fisicoquímicas Teóricas y Aplicadas; Argentin
Thermodynamic Theory of Multiresponsive Microgel Swelling
No full textUsing a thermodynamic theory, we present a systematic study of the behavior of microgels of N-isopropylacrylamide (NIPAm) and methacrylic acid (MAA) copolymers as a function of the temperature, pH, and salt concentration. These microgels swell with increasing pH; the onset of this transition displaces to higher pH values as the solution salt concentration decreases. The size of poly(NIPAm-co-MAA) microgels is a nonmonotonic function of the salt concentration; at constant pH, increasing the salt concentration drives particle swelling first, but a further increase of salinity leads to deswelling. Upon increasing the temperature, these microgels deswell and undergo a volume phase transition (VPT) around a characteristic temperature. This VPT temperature depends on the MAA content of the copolymer, the degree of cross-linking, the solution pH, and salt concentration. Changing these independent variables and/or design parameters are all means to modify the state of charge of the microgel at the VPT. The amount of the charge inside the polymer backbone controls the VPT temperature. Finally, we describe the absorption of two chemotherapeutic drugs, Daunorubicin and Doxorubicin, and evaluate the best conditions for incorporation into the multiresponsive microgels.Fil: Pérez Chávez, Néstor Ariel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Fisicoquímicas Teóricas y Aplicadas. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Instituto de Investigaciones Fisicoquímicas Teóricas y Aplicadas; ArgentinaFil: Albesa, Alberto Gustavo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Fisicoquímicas Teóricas y Aplicadas. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Instituto de Investigaciones Fisicoquímicas Teóricas y Aplicadas; ArgentinaFil: Longo, Gabriel Sebastian. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Fisicoquímicas Teóricas y Aplicadas. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Instituto de Investigaciones Fisicoquímicas Teóricas y Aplicadas; Argentin
Equilibrium Adsorption of Hexahistidine on pH-Responsive Hydrogel Nanofilms
Full text linkWe present a molecular theory to study the adsorption of different species within pH-sensitive hydrogel nanofilms. The theoretical framework allows for a molecular-level description of all the components of the system, and it explicitly accounts for the acid-base equilibrium. We concentrate in the adsorption of hexahistidine, one of the most widely used tags in bio-related systems, particularly in chromatography of proteins. The adsorption of hexahistidine within a grafted polyacid hydrogel film shows a non-monotonic dependence on the solution pH. Depending on the salt concentration, the density of the polymer network, and the bulk concentration of peptide, substantial adsorption is predicted in the intermediate pH range where both the network and the amino acids are charged. To enhance the electrostatic attractions, the acid-base equilibrium of adsorbed hexahistidine is shifted significantly increasing the degree of charge of the residues, as compared to the bulk solution. Such shift depends critically on the conditions of the environment at the nanoscale. At the same time, the degree of dissociation of the network becomes that of the isolated acid-group in a dilute solution, which means that the network is considerably more charged than when there is no adsorbate molecules. This work provides fundamental information on the physical chemistry behind the adsorption behavior and the response of the hydrogel film. This information can be useful in designing new materials for the purification or separation/immobilization of histidine-tagged proteins.Fil: Longo, Gabriel Sebastian. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico la Plata. Instituto de Investigaciones Fisicoquímicas Teóricas y Aplicadas; Argentina. Universidad Nacional de La Plata; ArgentinaFil: Olvera de la Cruz, Monica. Northwestern University; Estados UnidosFil: Szleifer, Igal. Northwestern University; Estados Unido
Investigating the Impact of Network Functionalization on Protein Adsorption to Polymer Nanogels
No full textThis study explores the impact of network functionalization and chemical composition on the pH-responsive behavior of polymer nanogels and their adsorption of proteins. Using a thermodynamic theory informed by a molecular model, this work evaluates the interactions of three proteins with varying isoelectric points (insulin, myoglobin, and cytochrome c) and pH-responsive nanogels based on methacrylic acid or allylamine motifs. Three different functionalization strategies are considered, with pH-responsive segments distributed randomly, at the center, or on the surface of the polymer network. Our results show that the spatial distribution of functional units affects both the nanogels’ mechanical response to pH changes and the level and localization of adsorbed proteins. The dependence of protein adsorption on the salt concentration is also investigated, with the conclusion that it is best to encapsulate proteins at low salt concentrations and aim for release at high salt concentrations. These results provide valuable information for the design of pH-responsive nanogels as vehicles for protein encapsulation, transport, and administration.Fil: Pérez Chávez, Néstor Ariel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Fisicoquímicas Teóricas y Aplicadas. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Instituto de Investigaciones Fisicoquímicas Teóricas y Aplicadas; ArgentinaFil: Albesa, Alberto Gustavo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Fisicoquímicas Teóricas y Aplicadas. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Instituto de Investigaciones Fisicoquímicas Teóricas y Aplicadas; ArgentinaFil: Longo, Gabriel Sebastian. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Fisicoquímicas Teóricas y Aplicadas. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Instituto de Investigaciones Fisicoquímicas Teóricas y Aplicadas; Argentin
Voltage induced adsorption of cationic nanoparticles on lipid membranes
No full textWe evaluate the effects of an applied electric potential on the adsorption/desorption mechanism of cationic nanoparticles on lipid membranes. By applying a molecular theory that allows calculating nanoparticle adsorption isotherms and free-energy profiles, we identify the conditions under which the external voltage promotes the adsorption of nanoparticles coated with cell penetrating peptides. We consider symmetric and asymmetric membranes made of neutral and acidic lipids and cover a wide range of environmental conditions (external voltage, pH, salt, and nanoparticles concentration) relevant to both electrochemical experiments and biological systems. For neutral membranes at low concentration of salt, a moderate external voltage (<100 mV) induces spontaneous adsorption of nanoparticles. For membranes containing a small fraction of anionic lipids, the external potential has little effect on the interfacial concentration of nanoparticles, and the membrane surface charge dominates the adsorption behavior. In all cases, the membrane-particle effective interactions, and its dependence on the external bias, are strongly modulated by the concentration of salt. At 100 mM NaCl, the external potential has almost no effect on the adsorption free energy profiles. In general, we provide a theoretical framework to evaluate the conditions under which nanoparticles are thermodynamically adsorbed or kinetically restrained to the vicinity of the membrane, and to assess the impact of the nanoparticles on the interfacial electrostatic properties.Fil: Chiarpotti, Maria Vanina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mendoza. Instituto Interdisciplinario de Ciencias Básicas. - Universidad Nacional de Cuyo. Instituto Interdisciplinario de Ciencias Básicas; ArgentinaFil: Longo, Gabriel Sebastian. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Fisicoquímicas Teóricas y Aplicadas. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Instituto de Investigaciones Fisicoquímicas Teóricas y Aplicadas; ArgentinaFil: del Popolo, Mario Gabriel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mendoza. Instituto Interdisciplinario de Ciencias Básicas. - Universidad Nacional de Cuyo. Instituto Interdisciplinario de Ciencias Básicas; Argentin
Molecular theory of glyphosate adsorption to pH-responsive polymer layers
Full text linkBy means of a molecular-level theory we investigate glyphosate adsorption from aqueous solutions to surface-grafted poly(allylamine) layers. Our molecular model of glyphosate and the polymeric material includes description of size, shape, conformational freedom, and state of protonation of both components. The composition of the bulk solution (pH, salt concentration and glyphosate concentration) plays a critical role to determine adsorption. Adsorption is a non-monotonic function of the solution pH, which can be explained in terms of the pH-dependent protonation behavior of both adsorbate and adsorbent material. Lowering the solution salinity is an efficient way to enhance glyphosate adsorption. This is because glyphosate and salt anions compete for adsorption to the polymer layer. In this competition, glyphosate deprotonation, to increase its negative charge upon entering the polymer layer, plays an critical role to favor its adsorption under a variety of solution conditions. This deprotonation is the result of the higher pH that establishes inside the polymer. Our results show that such pH increase can be controlled, while achieving significant glyphosate adsorption, through varying the grafting density of the material. This result is important since glyphosate degradation by microbial activity is pH-dependent. These polymeric systems are excellent candidates for the development functional materials that combine glyphosate sequestration and in situ biodegradation.Fil: Pérez Chávez, Néstor Ariel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Fisicoquímicas Teóricas y Aplicadas. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Instituto de Investigaciones Fisicoquímicas Teóricas y Aplicadas; ArgentinaFil: Albesa, Alberto Gustavo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Fisicoquímicas Teóricas y Aplicadas. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Instituto de Investigaciones Fisicoquímicas Teóricas y Aplicadas; ArgentinaFil: Longo, Gabriel Sebastian. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Fisicoquímicas Teóricas y Aplicadas. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Instituto de Investigaciones Fisicoquímicas Teóricas y Aplicadas; Argentin
How protonation modulates the interaction between proteins and pH-responsive hydrogel films
No full textHydrogels of pH-responsive polymers are promising candidates for the design of functional biomaterials. In this context, understanding the complexity of the interaction between these materials and proteins is essential. A recently developed molecular-level equilibrium theory for protein adsorption on hydrogels of cross-linked polyacid chains allows for modeling size, shape, charge distribution, protonation state and conformational degrees of freedom of all chemical species in the system; proteins are described using a coarse-grained model of their crystallographic structure. This review summarizes our recent studies, which have focused on understanding how the interaction between proteins and pH-responsive hydrogel films depends on the pH and salt concentration, both in single protein solutions and mixtures. In particular, we discuss the key role that protonation plays in mediating the polymer-protein electrostatic attractions that drive adsorption. Deprotonation of the polyacid network modifies the nano-environment inside the hydrogel; the local pH drops inside the film. In single protein solutions, protonation of amino acid residues in this lower-pH environment favors adsorption to the hydrogel. Upon adsorption, the net charge of the protein can be several units more positive than in the solution. The various amino acids protonate differently, in a non-trivial way, which gives flexibility to the protein to enhance its positive charge and favor adsorption under a wide range of conditions. In binary and ternary protein solutions, amino acid protonation is the decisive factor for selective adsorption under certain conditions. We show that the polymer network composition and the solution pH can be used to separate and localize proteins within nanometer-sized regions.Fil: Longo, Gabriel Sebastian. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Fisicoquímicas Teóricas y Aplicadas. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Instituto de Investigaciones Fisicoquímicas Teóricas y Aplicadas; ArgentinaFil: Pérez Chávez, Néstor Ariel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Fisicoquímicas Teóricas y Aplicadas. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Instituto de Investigaciones Fisicoquímicas Teóricas y Aplicadas; ArgentinaFil: Szleifer, Igal. Northwestern University; Estados Unido
Lysozyme adsorption in pH-responsive hydrogel thin-films: the non-trivial role of acid-base equilibrium
Full text linkWe develop and apply a molecular theory to study the adsorption of lysozyme on weak polyacid hydrogel films. The theory explicitly accounts for the conformation of the network, the structure of the proteins, the size and shape of all the molecular species, their interactions as well as the chemical equilibrium of each titratable unit of both the protein and the polymer network. The driving forces for adsorption are the electrostatic attractions between the negatively charged network and the positively charged protein. The adsorption is a non-monotonic function of the solution pH, with a maximum in the region between pH 8 and 9 depending on the salt concentration of the solution. The non-monotonic adsorption is the result of increasing negative charge of the network with pH, while the positive charge of the protein decreases. At low pH the network is roughly electroneutral, while at sufficiently high pH the protein is negatively charged. Upon adsorption, the acid-base equilibrium of the different amino acids of the protein shifts in a nontrivial fashion that depends critically on the particular kind of residue and solution composition. Thus, the proteins regulate their charge and enhance adsorption under a wide range of conditions. In particular, adsorption is predicted above the protein isoelectric point where both the solution lysozyme and the polymer network are negatively charged. This behavior occurs because the pH in the interior of the gel is significantly lower than that in the bulk solution and it is also regulated by the adsorption of the protein in order to optimize protein-gel interactions. Under high pH conditions we predict that the protein changes its charge from negative in the solution to positive within the gel. The change occurs within a few nanometers at the interface of the hydrogel film. Our predictions show the non-trivial interplay between acid-base equilibrium, physical interactions and molecular organization under nanoconfined conditions, which leads to non-trivial adsorption behavior that is qualitatively different from what would be predicted from the state of the proteins in the bulk solution.Fil: Narambuena, Claudio Fabian. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Fisicoquímicas Teóricas y Aplicadas. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Instituto de Investigaciones Fisicoquímicas Teóricas y Aplicadas; Argentina. Northwestern University; Estados UnidosFil: Longo, Gabriel Sebastian. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Fisicoquímicas Teóricas y Aplicadas. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Instituto de Investigaciones Fisicoquímicas Teóricas y Aplicadas; ArgentinaFil: Szleifer, Igal. Northwestern University; Estados Unido
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