Do properties of bovine serum albumin at fluid/electrolyte interface follow the Hofmeister series?—An analysis using Langmuir and Langmuir–Blodgett films

Lakshmanan, Muthuselvi; Parthasarathi, Ramakrishnan; Dhathathreyan, Aruna

doi:10.1016/j.bbapap.2006.09.010

Cited by 12 publications

(5 citation statements)

References 47 publications

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“…It has been reported by Lakshmanan et al in the case of BSA, that the percentage of helicity, which is a measure of compactness and folding of protein, increases in the presence of different electrolytes. 81 It has also been reported that Hb dissociated from a tetramer to a dimer in the presence of an inorganic salt, as revealed from light scattering experiments as well as sedimentation velocity measurements. 33,34 The dissociation of glucose oxidase (GOX) is also reported in presence of ionic strength by neutron reflectivity experiments.…”

Section: Ion-protein Interaction and Relevance To Dlvo Theorymentioning

confidence: 87%

Influence of KCl on the interfacial activity and conformation of hemoglobin studied by Langmuir–Blodgett technique

Mahato

Pal

Kamilya

et al. 2010

Phys. Chem. Chem. Phys.

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We report here the influence of KCl on the interfacial surface activity and conformation of human adult hemoglobin (Hb) using Langmuir and Langmuir-Blodgett (LB) techniques. The studies were done in absence and in presence of KCl salt in the subphase. We have studied the surface pressure-area (π-A) isotherm and surface pressure-time (π-t) kinetics of Hb with the variation of KCl concentrations (C(KCl)). The π-t study shows that the surface activity as well as the magnitude of diffusion and rearrangement of Hb at air/water interface is a function of C(KCl). Conformational study was done by CD spectroscopy and by the FTIR technique. Both the studies show an increasing trend of the α-helix form of Hb in the presence of KCl which may be responsible for the increased surface activity of Hb. The free energy calculations show that the compression of the Hb monolayer is involved in the small free energy change (∼5-25 kcal mol(-1)) of Hb. The changes in area per molecule and free energy, as well as other results, indicate that the influence of KCl on the Hb monolayer is in line with modified DLVO theory of ion-protein interaction. FE-SEM study shows that the LB films in absence of KCl comprise higher aggregates, whereas in the presence of KCl (0.5 M) it comprises lower aggregates, indicating the structural change of Hb. KCl salt here enhances the α-helix from of Hb, promoting the folded conformation by perturbing the water structure. The overall results show that the intermolecular forces and the surface activity as well as the population of the α-helix of Hb can be tuned by KCl salt.

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Section: Ion-protein Interaction and Relevance To Dlvo Theorymentioning

confidence: 87%

Influence of KCl on the interfacial activity and conformation of hemoglobin studied by Langmuir–Blodgett technique

Mahato

Pal

Kamilya

et al. 2010

Phys. Chem. Chem. Phys.

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“…In addition to liquid viscosity and density, temperature and pressure (Shen et al , 2008), signals can be affected by electrode surface roughness and wetability (Cho et al ., 2007b; Roach et al , 2007; Zhuang et al , 2007), compressional wave reflection from a liquid meniscus in an open well or immersion configuration (Picard and Davoust, 2007; Shen et al ., 2007a), hydrostatic pressure in a flow system (Ogi et al , 2008), liquid permittivity and conductivity (Yu and Janata, 2008), particularly if the electrode/circuit is not well grounded (Yoshimoto et al , 2006), shear oscillation amplitutde (Edvardsson et al , 2006; Encarnacao et al , 2007; Yoshimoto et al , 2007), and a variety of properties of the bound layer; shear modulus and elasticity(Jimenez et al , 2006; Rojas et al , 2008), homogeneity, topology and viscosity. Explanations for ‘missing mass’ centre on discussions of ‘coupled water’ (Lakshmanan et al , 2006; Bingen et al , 2008; Wang et al ., 2008a; Furusawa et al , 2009b), the geometry and homogeneity of the attachmed mass on the surface (Konig et al , 2006; Johannsmann et al , 2008; Johannsmann et al , 2009; Tellechea et al , 2009), and various interpretations of the impact of the viscoelastic properties of the interfacial layer (Dutta et al , 2008; Johannsmann, 2008; Zhu et al , 2008; Zhuang et al , 2008; Furusawa et al ., 2009a; Patel et al ., 2009b).…”

Section: Theorymentioning

confidence: 99%

A survey of the 2006–2009 quartz crystal microbalance biosensor literature

Becker

Cooper

2011

J of Molecular Recognition

163

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Since the publication of the original review of piezoelectric acoustic sensors in this series there has been a consistent, gradual expansion in the number of published papers using 'quartz crystal microbalances' (QCM). Between 2001 and 2009, the number of QCM publications per annum has increased from 49 to 273, with a two-fold increase in papers per annum between 2004 and 2008. Within the field, comparing the time covered by the current to the previous review, there are trends towards increasing use of QCM in the study of protein adsorption to surfaces (93% increase), homeostasis (67% increase), protein-protein interactions (40% increase) and carbohydrates (43% increase). New commercial systems have been released that are driving the uptake of the technology for characterization of binding specificities, affinities, kinetics and conformational changes associated with a molecular recognition event. This paper highlights theoretical and practical aspects of the principles that underpin acoustic analysis, then reviews exemplary papers in key application areas involving small molecular weight ligands, carbohydrates, proteins, nucleic acids, viruses, bacteria, cells and membrane interfaces.

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“…Hofmeister ions are generally known to exert their effects indirectly by changing the hydrogen-bonding properties of water. The question of how Hofmeister ions affect the structure and hydrogen-bonding properties of water has been reviewed by Collins and Washabaugh and the problem is being actively investigated today by many research groups. − Surface viscoelasticity is also one of the main factors controlling the mechanical behavior of the protein solution as a whole under shear. Although there has been ongoing research on the relation between surface rheology and bulk rheology, , the rheological behavior of protein films is still an area that is not fully understood from either the experimental or modeling points of view.…”

Section: Introductionmentioning

confidence: 99%

Assembling Fibrinogen at Air/Water and Solid/Liquid Interfaces Using Langmuir and Langmuir−Blodgett Films

Sankaranarayanan¹,

Dhathathreyan²,

Miller

2010

J. Phys. Chem. B

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Langmuir films of pure fibrinogen (Fg) and Fg spread at the air/buffer interface and subphase containing electrolytes, NaCl, KCl, CaCl(2), and ZnCl(2), have been analyzed to understand the role of the surface/interface in mediating the organization of the protein eventually to fibrils. These films have been characterized by the surface pressure and surface potential-molecular area ((pi-A) and (DeltaV-A)) isotherms and Brewster angle microscopy (BAM). The Langmuir-Blodgett (LB) films of the protein transferred to the solid substrates have been characterized by scanning electron microscopy (SEM) and circular dichroism (CD). Our results suggest that fibrils are formed during organization at air/solution interface and also in LB films. The rate of formation of the fibril is the maximum for Fg with ZnCl(2). Adsorption of Fg to surfaces coated with a neutral lipid, dimyristoylphosphatidylcholine (DMPC), and a cationic lipid, dioctadecyldimethylammonium bromide (DOMA), from a range of solution concentrations has been studied using a quartz crystal microbalance (QCM). The work of adhesion of the protein on the solid surface shows fibril formation and positive adhesion for Fg in the presence of electrolytes. SEM results show that the adherent protein exhibits the widely reported nodulelike structure in the presence of CaCl(2) and ZnCl(2). These results provide definite evidence that specifically designed surfaces can promote adhesion of Fg and also activate fibril formation even in the absence of thrombin.

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Do properties of bovine serum albumin at fluid/electrolyte interface follow the Hofmeister series?—An analysis using Langmuir and Langmuir–Blodgett films

Cited by 12 publications

References 47 publications

Influence of KCl on the interfacial activity and conformation of hemoglobin studied by Langmuir–Blodgett technique

Influence of KCl on the interfacial activity and conformation of hemoglobin studied by Langmuir–Blodgett technique

A survey of the 2006–2009 quartz crystal microbalance biosensor literature

Assembling Fibrinogen at Air/Water and Solid/Liquid Interfaces Using Langmuir and Langmuir−Blodgett Films

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