Adsorption of Globular Proteins at the Air/Water Interface as Measured via Dynamic Surface Tension: Concentration Dependence, Mass-Transfer Considerations, and Adsorption Kinetics

Tripp, Brian C.; Magda, Jules J.; Andrade, Joseph D.

doi:10.1006/jcis.1995.1291

Cited by 218 publications

(208 citation statements)

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“…Determination of surface tension by axisymmetric drop shape analysis is a well-established and accurate technique, enabling recording of the entire dynamic surfactant behavior without any restrictions (e.g. drop shape or size and liquid meniscus contact angle) and has been described previously (31)(32)(33). At least three independent assays were performed, with each drop done in duplicate.…”

Section: Methodsmentioning

confidence: 99%

Combined Effects of Agitation, Macromolecular Crowding, and Interfaces on Amyloidogenesis

Lee

Bird

Shaw

et al. 2012

Journal of Biological Chemistry

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Background: Macromolecular crowding and hydrophobic-hydrophilic interfaces promote amyloidogenesis. Results: The outcome of macromolecular crowding on A␤ amyloidogenesis depends on the spatial heterogeneity of the system. Conclusion: Viscosity dominates over the excluded volume effect only when the system contains a hydrophobic-hydrophilic interface. Significance: Studying both interfacial and macromolecular crowding effects together is crucial to understand amyloid systems in a physiological context.

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Section: Methodsmentioning

confidence: 99%

Combined Effects of Agitation, Macromolecular Crowding, and Interfaces on Amyloidogenesis

Lee

Bird

Shaw

et al. 2012

Journal of Biological Chemistry

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“…The fundamental equilibrium adsorption equation for a two component system (solvent component "1", solute component "2"; water and protein, respectively) according to the Guggenheim surface construction [28,29] reads: (4) where γ is interfacial tension (ergs/cm 2 = mJ/m 2 ), Γ ≡ (n I / A) measures the number of moles within the interphase n I per-unit-area (moles/cm 2 ), and n B is the mole number within bulk solution. At equilibrium, the solute chemical potential μ 2 in bulk solution is equal to that within the interphase so that ; where A is solute activity and B or I denotes bulk phase or interphase, respectively.…”

Section: Appendix B1mentioning

confidence: 99%

“…By contrast, the interfacial tensions that are exquisitely-sensitive measures of surfactant adsorption are observed to decay over tens-of-minutes or even hours (see refs. [4][5][6][7][8][9][10][11] for recent work on a broad selection of purified blood proteins as well as serum derived from different species).…”

Section: Introductionmentioning

confidence: 99%

Volumetric interpretation of protein adsorption: Kinetic consequences of a slowly-concentrating interphase

Barnthip¹,

Noh²,

Leibner³

et al. 2008

Biomaterials

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Time-dependent energetics of blood-protein adsorption are interpreted in terms of a slowlyconcentrating three-dimensional interphase volume initially formed by rapid diffusion of protein molecules into an interfacial region spontaneously formed by bringing a protein solution into contact with a physical surface. This modification of standard adsorption theory is motivated by the experimental observation that interfacial tensions of protein-containing solutions decrease slowly over the first hour to a steady-state value while, over this same period, the total adsorbed-protein mass is constant (for lysozyme, 15 kDa; albumin, 66 kDa; prothrombin, 72 kDa; IgG, 160 kDa; fibrinogen, 341 kDa studied in this work). These seemingly divergent observations are rationalized by the fact that interfacial energetics (tensions) are explicit functions of solute chemical potential (concentration), not adsorbed mass. Hence, rates-of-interfacial-tension-change parallel a slow interphase concentration effect whereas solution depletion detects a constant interphase composition within the time frame of experiment. A straightforward mathematical model approximating the perceived physical situation leads to an analytic formulation that is used to compute time-varying interphase volume and protein concentration from experimentally-measured interfacial tensions. Derivation from the fundamental thermodynamic adsorption equation verifies that protein adsorption from dilute solution is controlled by a partition coefficient at equilibrium, as is observed experimentally at steady state. Implications of the alternative interpretation of adsorption kinetics on biomaterials and biocompatibility are discussed. KeywordsProtein adsorption; kinetics; interfacial energetics; interphase; surface; radiometry IntroductionProtein-adsorption kinetics are of practical importance in biomaterials because adsorption rates have been implicated as a cause of selective protein adsorption. For example, the so-called Vroman Effect is commonly thought to occur because low-molecular-weight proteins *Author to whom correspondence should be addressed EAV3@PSU.EDU. Publisher's Disclaimer: 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 citable 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. NIH Public Access Author ManuscriptBiomaterials. Author manuscript; available in PMC 2009 July 1. Published in final edited form as:Biomaterials. presumably arriving first at a surface immersed in a multi-component solution are displaced by higher-molecular-weight proteins arriving later (see refs. and citations therein). The final adsorbed-protein composition is thus purported to be achieved through a complex se...

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“…The general accepted behavior is that the proteins lose their native biological activities when exposed to the air-water interface or when interacting with the lipid monolayer by changing their secondary structures [28]. It is also a well-accepted phenomenon that the protein's adsorption kinetics is a nonlinear process and the interfacial pressure reaches a plateau within a certain time after the injection into the subphase.…”

Section: Lipid Solution and Monolayer Preparation 23 Lipoprotein Solmentioning

confidence: 99%

Adsorption kinetics of low-density lipoproteins with Langmuir monolayer

Khattari

2016

J Biol Phys

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The present work utilizes the Langmuir monolayer technique to detect the adsorption kinetics of native low-density lipoproteins and their oxidized form with the lipid monolayer. We found that low-density lipoproteins and oxidized low-density lipoproteins are able to penetrate the LM up to pressure π = 9.9 and 11.6 mN/m. Also, the adsorption constants of both particles were found to depend strongly on the monolayer initial pressure. It is found that less compressed lipid monolayers could accommodate more native low-density lipoproteins than the oxidized ones due their higher binding affinity toward monolayers. The probable α-helical regions along the apoproteinB-100 secondary structure and average hydrophobicity could explain partially their adsorption kinetics into lipid monolayers. This simplified 'in vitro' study of low-density lipoproteinmonolayer interaction may serve as a step further to understand the mechanism and bioactivity of the atherosclerotic process. Also, it may shed light on the oxidized low-density lipoprotein's role in plaque formation in the innermost arterial wall in blood vessels. Keywords Langmuir monolayer . Atherosclerosis . LDL oxidation . Adsorption kineticsAtherosclerosis is a complex chronically developing human disease initiated by and progressing as a result of excessive accumulation of lipids (e.g., mostly cholesterol in human blood) in the smooth arterial wall [1][2][3]. Cardiovascular disease is first distinguishable by a fatty streak, which is lipid-rich macrophages and T lymphocytes trapped by the artery wall (i.e., intima) [4]. As oxidization continues, fatty steaks decompose to polyunsaturated

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Adsorption of Globular Proteins at the Air/Water Interface as Measured via Dynamic Surface Tension: Concentration Dependence, Mass-Transfer Considerations, and Adsorption Kinetics

Cited by 218 publications

References 0 publications

Combined Effects of Agitation, Macromolecular Crowding, and Interfaces on Amyloidogenesis

Combined Effects of Agitation, Macromolecular Crowding, and Interfaces on Amyloidogenesis

Volumetric interpretation of protein adsorption: Kinetic consequences of a slowly-concentrating interphase

Adsorption kinetics of low-density lipoproteins with Langmuir monolayer

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