Human Immunoglobulin Adsorption Investigated by Means of Quartz Crystal Microbalance Dissipation, Atomic Force Microscopy, Surface Acoustic Wave, and Surface Plasmon Resonance Techniques

Zhou, Cheng; Friedt, Jean‐Michel; Angelova, Angelina; Choi, Kang‐Hoon; Laureyn, Wim; Frederix, Filip; Francis, Laurent; Campitelli, Andrew; Engelborghs, Yves; Borghs, Gustaaf

doi:10.1021/la036251d

Cited by 162 publications

(174 citation statements)

References 59 publications

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“…The adsorbed mass for both proteins is consistent with an adsorbed monolayer [15,38,39]. Based on a protein density of 1.15 g cm -3 [15] , the thickness of the layers on silica at pH 7.4 would be 16.8 nm for BGG and 5.1 nm for BSA which is consistent with the protein dimensions if proteins adsorbed with an end-on orientation [15,38].…”

Section: Protein Layer Formed In Single Protein Bsa Solutions and Bgsupporting

confidence: 63%

Synovial Fluid Lubrication: The Effect of Protein Interactions on Adsorbed and Lubricating Films

et al. 2015

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Section: Protein Layer Formed In Single Protein Bsa Solutions and Bgsupporting

confidence: 63%

Synovial Fluid Lubrication: The Effect of Protein Interactions on Adsorbed and Lubricating Films

et al. 2015

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“…In other words, the interface (interphase) should properly regarded as a volume comprised of both 2D surface and subsurface region -not just 2D surface alone. This distinction between 2D and 3D becomes particularly important in the event of multilayer adsorption, as has been shown to occur for proteins by a number of investigators using a variety of experimental methods over the last twenty years or so [5,6,10,22,24,26,[55][56][57][58][59][60][61][62][63][64].A primary issue with the 2D model applied to the interpretation of principal observations (i) and (ii) of the preceding section is that it eliminates an important degree-of-freedom that allows adsorbate concentration to vary independent of adsorbed mass. Partly because of this, we suspect, modern embellishments of RSA theory are forced to embrace an ever-increasing number of variables to explain all experimental outcomes (see, as a recent example, ref.…”

mentioning

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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“…At a density of 617 ng/cm 2 , the HSP70 antibody appears to have formed a complete monolayer on the SAM, as similar immunoglobulin G (IgG) proteins have reported monolayer a 200-550 ng/cm 2 mass density. 36 The mass density depends on the orientation of the antibody, with flat-on orientation resulting in lower densities and end-on resulting in higher densities. 36 This indicates that the HSP70 antibody layer is densely packed with an end-on orientation, and the large protein binding density indicates that the antibody remains highly active while bound to the sensor surface.…”

Section: Experimental Setup and Resultsmentioning

confidence: 99%

Enhancing conjugation rate of antibodies to carboxylates: Numerical modeling of conjugation kinetics in microfluidic channels and characterization of chemical over-exposure in conventional protocols by quartz crystal microbalance

2015

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This research reports an improved conjugation process for immobilization of antibodies on carboxyl ended self-assembled monolayers (SAMs). The kinetics of antibody/SAM binding in microfluidic heterogeneous immunoassays has been studied through numerical simulation and experiments. Through numerical simulations, the mass transport of reacting species, namely, antibodies and crosslinking reagent, is related to the available surface concentration of carboxyl ended SAMs in a microchannel. In the bulk flow, the mass transport equation (diffusion and convection) is coupled to the surface reaction between the antibodies and SAM. The model developed is employed to study the effect of the flow rate, conjugating reagents concentration, and height of the microchannel. Dimensionless groups, such as the Damk€ ohler number, are used to compare the reaction and fluidic phenomena present and justify the kinetic trends observed. Based on the model predictions, the conventional conjugation protocol is modified to increase the yield of conjugation reaction. A quartz crystal microbalance device is implemented to examine the resulting surface density of antibodies. As a result, an increase in surface density from 321 ng/cm 2 , in the conventional protocol, to 617 ng/cm 2 in the modified protocol is observed, which is quite promising for (bio-) sensing applications. Microfluidics have been implemented in various bio-medical diagnostic applications, such as immunosensors and molecular diagnostic devices. 1 In the last decade, a vast number of biochemical species has been detected by microfluidic-based immunosensors. Immunosensors are sensitive transducers which translate the antibody-antigen reaction to physical signals. The detection in an immunosensor is performed through immobilization of an antibody that is specific to the analyte of interest. 2 The antibody is often bound to the transducing surface of the sensor covered by selfassembled monolayers (SAMs). SAMs are organic materials that form a thin, packed and robust interface on the surface of noble metals like that of gold, suitable for biosensing applications. 3 Thiolic SAMs have a "head" group that shows a high affinity to being chemisorbed onto a substrate, typically gold. The SAMs' carboxylic functional group of the "tail" end can be linked to an amine terminal of an antibody to form a SAM/antibody conjugation. 3,4 The conjugation process is usually accomplished in the presence of carbodiimides, such as 1-ethyl-3-(3-dimethylaminopropyl) carbodiimide (EDC). A yield increasing additive, N-Hydroxysuccinimide (NHS), is often used to enhance the surface loading density of the antibody. 4,5 a) S. Asiaei, B. Smith, and P. Nieva contributed equally to this work. b)

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Human Immunoglobulin Adsorption Investigated by Means of Quartz Crystal Microbalance Dissipation, Atomic Force Microscopy, Surface Acoustic Wave, and Surface Plasmon Resonance Techniques

Cited by 162 publications

References 59 publications

Synovial Fluid Lubrication: The Effect of Protein Interactions on Adsorbed and Lubricating Films

Synovial Fluid Lubrication: The Effect of Protein Interactions on Adsorbed and Lubricating Films

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

Enhancing conjugation rate of antibodies to carboxylates: Numerical modeling of conjugation kinetics in microfluidic channels and characterization of chemical over-exposure in conventional protocols by quartz crystal microbalance

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