The Adsorption and Conformation of Plasma Proteins: A Physical Approach*

Morrissey, B. W.

doi:10.1111/j.1749-6632.1977.tb41752.x

Cited by 178 publications

(49 citation statements)

References 30 publications

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“…extensively studied (32)(33)(34)(35)(36)(37)(38). It has been reported that conformational changes or rearrangements of fibrinogen or HSA Although still unresolved, it appears that particular protein conformations contribute differently to calcium binding and molecules upon adsorption are considerable and increase with time on the surface (37-39).…”

Section: Resultsmentioning

confidence: 99%

The Dual Role of Fibrinogen as Inhibitor and Nucleator of Calcium Phosphate Phases: The Importance of Structure

Tsortos

Ohki

Zieba

et al. 1996

Journal of Colloid and Interface Science

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Section: Resultsmentioning

confidence: 99%

The Dual Role of Fibrinogen as Inhibitor and Nucleator of Calcium Phosphate Phases: The Importance of Structure

Tsortos

Ohki

Zieba

et al. 1996

Journal of Colloid and Interface Science

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“…This structural heterogeneity is explained by the altered conditions experienced by proteins that arrive late at the interface during the adsorption process (18)(19)(20)(21). Protein molecules that arrive first at the interface have sufficient space to adapt to the interface, allowing conformational changes like expansion to a molten globule to occur.…”

Section: Resultsmentioning

confidence: 99%

Conformation and orientation of a protein folding intermediate trapped by adsorption

Engel

Visser

Mierlo

2004

Proc. Natl. Acad. Sci. U.S.A.

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Although adsorption-induced conformational changes of proteins play an essential role during protein adsorption on interfaces, detailed information about these changes is lacking. To further the current understanding of protein adsorption, in this study, the orientation, conformation, and local stability of bovine ␣-lactalbumin (BLA) adsorbed on polystyrene nanospheres is characterized at the residue level by hydrogen͞deuterium exchange and 2D NMR spectroscopy. Most of the adsorbed BLA molecules have conformational properties similar to BLA molecules in the acid-induced molten globule state (A state). A folding intermediate of BLA is thus induced and trapped by adsorption of the protein on the hydrophobic interface. Several residues, clustered on one side of the adsorbed folding intermediate of BLA, have altered amide proton exchange protection factors compared to those of the A state of BLA. This side preferentially interacts with the interface and includes residues in helix C, the calcium binding site, and part of the ␤-domain. Local unfolding of this interacting part of the adsorbed protein seems to initiate the adsorption-induced unfolding of BLA. Adsorption-induced protein unfolding apparently resembles more the mechanical unfolding of a protein than the global unfolding of a protein as induced by denaturant, pH, or pressure. 2D macromolecular crowding prevented the minority of adsorbed BLA molecules, which arrived late at the interface, to unfold to the A state. Protein adsorption is a novel and challenging approach to probe features of the free energy landscapes accessible to unfolding proteins.bovine ␣-lactalbumin ͉ hydrogen͞deuterium exchange ͉ NMR A dsorption of protein molecules on solid interfaces is important in fields like biomedical materials engineering (1), chromatography (2), and nanotechnology (3, 4). To understand protein adsorption, knowledge of adsorption-induced conformational changes of proteins is essential (5, 6). Unfortunately, because of considerable experimental difficulties, detailed information at the submolecular level about these conformational changes is sparse (7-12), which hampers the further development of the theory of protein adsorption. To stimulate this development, we characterize here at the residue level, the orientation, conformation, and local stability of bovine ␣-lactalbumin (BLA) adsorbed on polystyrene nanospheres by hydrogen͞deuterium (H͞D) exchange and 2D NMR spectroscopy. BLA, a 14-kDa protein from milk, is chosen to study protein adsorption because its structure, stability, and folding behavior have been thoroughly investigated. In addition, the adsorption of BLA on a variety of interfaces has been studied.Information about the stability and dynamics of a protein at the level of single amino acids can be obtained by investigating its H͞D exchange characteristics (13). In this study, BLA molecules in the native state are added to solid polystyrene nanospheres in 2 H 2 O. All added protein molecules adsorb spontaneously and rapidly [i.e., within 15 ms (14)] on ...

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“…[4] were estimated statistically by a data-fitting procedure based on a nonlinear least-squares regression method. Figure 1 shows typical desorption curves of BSA from Al 2 O 3 surfaces at different θ , where ln was plotted against the elution time (τ unit).…”

Section: Modelingmentioning

confidence: 99%

“…In general, the initial attachment of proteins onto a solid surface is affected by the intrinsic properties of proteins, solution conditions, and solid-surface properties (1). Proteins are known to undergo changes in conformation (surface-induced and time-dependent) upon adsorption (1-3) and coexist in different orientations, e.g., end-on and side-on configuration, on a contact surface, depending on protein concentration (4,5). A more flattened configuration can enhance the opportunity of multiple bonds with the surface, resulting in a strong interaction.…”

Section: Introductionmentioning

confidence: 99%

Kinetic Study of Desorption of Two Species of Bovine Serum Albumin from Alumina during Alkali Elution Process

Urano

Fukuzaki

2002

Journal of Colloid and Interface Science

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The Adsorption and Conformation of Plasma Proteins: A Physical Approach*

Cited by 178 publications

References 30 publications

The Dual Role of Fibrinogen as Inhibitor and Nucleator of Calcium Phosphate Phases: The Importance of Structure

The Dual Role of Fibrinogen as Inhibitor and Nucleator of Calcium Phosphate Phases: The Importance of Structure

Conformation and orientation of a protein folding intermediate trapped by adsorption

Kinetic Study of Desorption of Two Species of Bovine Serum Albumin from Alumina during Alkali Elution Process

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