About the albumin structure in solution: cigar Expanded form versus heart Normal shape

Leggio, Claudia; Galantini, Luciano; Pavel, Nicolae Viorel

doi:10.1039/b808938h

Cited by 74 publications

(82 citation statements)

References 63 publications

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“…These values for the spheroid semi-axes are in good accord with previously reported values, and in reasonable agreement with the linear dimensions of the reported heart-shape like crystal structure of albumins [28][29][30]32]. In a related, recent study by part of the present authors [9], similar values a = 1.80 ± 0.05 nm and b = 4.60 ± 0.15 nm have been determined, which are in decent agreement with the values obtained here.…”

Section: Static Properties: Experiments and Theorysupporting

confidence: 81%

“…I(q) ∝ P (q). Crystallographic measurements [28][29][30] have revealed a flat and roughly heartshaped structure of albumins. The computation of singleparticle properties with an account of the highly complex particle shape of biomolecules can be done by numerical simulations only and is beyond the scope of this paper [29,31].…”

Section: Single-particle Propertiesmentioning

confidence: 99%

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Viscosity and diffusion: crowding and salt effects in protein solutions

et al. 2012

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We report on a joint experimental-theoretical study of collective diffusion in, and static shear viscosity of solutions of bovine serum albumin (BSA) proteins, focusing on the dependence on protein and salt concentration. Data obtained from dynamic light scattering and rheometric measurements are compared to theoretical calculations based on an analytically treatable spheroid model of BSA with isotropic screened Coulomb plus hard-sphere interactions. The only input to the dynamics calculations is the static structure factor obtained from a consistent theoretical fit to a concentration series of small-angle X-ray scattering (SAXS) data. This fit is based on an integral equation scheme that combines high accuracy with low computational cost. All experimentally probed dynamic and static properties are reproduced theoretically with an at least semi-quantitative accuracy. For lower protein concentration and low salinity, both theory and experiment show a maximum in the reduced viscosity, caused by the electrostatic repulsion of proteins. The validity range of a generalized Stokes-Einstein (GSE) relation connecting viscosity, collective diffusion coefficient, and osmotic compressibility, proposed by Kholodenko and Douglas [PRE, 1995[PRE, , 51, 1081 is examined. Significant violation of the GSE relation is found, both in experimental data and in theoretical models, in semi-dilute systems at physiological salinity, and under low-salt conditions for arbitrary protein concentrations.

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Section: Static Properties: Experiments and Theorysupporting

confidence: 81%

Section: Single-particle Propertiesmentioning

confidence: 99%

Viscosity and diffusion: crowding and salt effects in protein solutions

et al. 2012

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“…In the samples without denaturant, the values of HSA do not show significant changes when the ibuprofen is added, and an R h value, in agreement with that reported in literature for free albumins, is observed. 45,53,54 Starting from this value, by increasing the denaturant concentration, an increment of the protein size is observed.…”

Section: Comparison Between Saxs and Dlsmentioning

confidence: 99%

Human serum albumin binding ibuprofen: A 3D description of the unfolding pathway in urea

Galantini¹,

Leggio²,

Konarev³

et al. 2010

Biophysical Chemistry

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This is a PDF file of an unedited manuscript that has been accepted for publication. As a service to our customers we are providing this early version of the manuscript. The manuscript will undergo copyediting, typesetting, and review of the resulting proof before it is published in its final form. Please note that during the production process errors may be discovered which could affect the content, and all legal disclaimers that apply to the journal pertain. A C C E P T E D M A N U S C R I P T ACCEPTED MANUSCRIPT A C C E P T E D M A N U S C R I P T ACCEPTED MANUSCRIPT2 AbstractSmall angle X-ray scattering (SAXS) technique, supported by light scattering measurements and spectroscopic data (circular dichroism and fluorescence) allowed us to restore the 3D structure at low resolution of defatted human serum albumin (HSA) in interaction with ibuprofen. The data were carried out on a set of HSA solutions with urea concentrations between 0.00 and 9.00 M. The SingularValue Decomposition method, applied to the complete SAXS data set allowed us to distinguish three different states in solution. In particular a native conformation N (at 0.00 M urea), an intermediate I1(at 6.05 M urea) and an unfolded structure U (at 9.00 M urea) were recognized. The low resolution structures of these states were obtained by exploiting both ab initio and rigid body fitting methods. In particular, for the protein without denaturant, a conformation recently described (Leggio & al., PCCP, 2008, 10, 6741-6750), very similar to the crystallographic heart shape, with only a slight reciprocal movement of the three domains, was confirmed. The I1 structure was instead characterized by only a closed domain (domain III) and finally, the recovered structure of the U state revealed the characteristic feature of a completely open state. A direct comparison with the free HSA pointed out that the presence of the ibuprofen provokes a shift of the equilibrium towards higher urea concentrations without changing the unfolding sequence. The work represents a type of analysis which could be exploited in future investigations on proteins in solution, in the binding of drugs or endogenous compounds and in the pharmacokinetic properties as well as in the study of allosteric effects, cooperation or anticooperation mechanisms.

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“…In contrast BSA is structurally unstable (''soft'') protein and undergoes very easily pH dependent conformational changes [10,11]. FIB consists of three domains which can change their conformation or their relative orientation in the adsorption process depending on different parameters.…”

mentioning

confidence: 97%

Initial bioadhesion on medical glass packaging materials investigated by dynamic contact angle measurements

Köhler

Müller

Hermsdörfer

et al. 2013

Physica Status Solidi (a)

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Glass is one of the most important materials in medical packaging. Protein adsorption at the glass walls leads to loss of the active substance in the glass vials and thus to high costs for the pharmaceutical industry, in particular in the case of expensive drugs. Thus more knowledge about the basic mechanisms and the involved parameters in protein interaction with glass surfaces is desirable. In this context, the adsorption of bovine serum albumin (BSA), fibrinogen (FIB), and lysozyme (LYS) on typical glass surfaces (borosilicate glass, quartz glass) was investigated by dynamic contact angle (DCA) measurements as a function of pH value. DCA allows the determination of the relative amount of adsorbed protein and of the reversibility of the adsorption process. It will be shown that the amount of adsorbed protein is governed by electrostatics on quartz glass while on borosilicate glass no influence of the pH value (and hence the electrostatics) can be seen. This can be explained by the different surface composition which has apparently an important influence on the adsorption process. In addition it could be determined that on both glass surfaces, none of the investigated proteins shows a complete reversibility of the adsorption process, i.e., desorption is never complete. In conclusion the interaction with glass surfaces cannot be generalized but electrostatics play a major role and thus the interaction of proteins with glass surfaces may be changed by shifting the pH value of the solutions or the isoelectric point (IEP) of the surfaces.

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About the albumin structure in solution: cigar Expanded form versus heart Normal shape

Cited by 74 publications

References 63 publications

Viscosity and diffusion: crowding and salt effects in protein solutions

Viscosity and diffusion: crowding and salt effects in protein solutions

Human serum albumin binding ibuprofen: A 3D description of the unfolding pathway in urea

Initial bioadhesion on medical glass packaging materials investigated by dynamic contact angle measurements

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