The Vroman effect: Competitive protein exchange with dynamic multilayer protein aggregates

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Title: The Vroman effect: Competitive protein exchange with dynamic multilayer protein aggregates
Authors: Hirsh, Stacey L., McKenzie, David R., Nosworthy, Neil J., Denman, John A., Sezerman, Uğur, Bilek, Marcela M. M.
Contributors: Hirsh, Stacey L, McKenzie, David R, Nosworthy, Neil J, Denman, John A, Sezerman, Osman U, Bilek, Marcela MM
Source: Colloids and Surfaces B: Biointerfaces. 103:395-404
Publisher Information: Elsevier BV, 2013.
Publication Year: 2013
Subject Terms: Time Factors, 02 engineering and technology, Microscopy, Atomic Force, Models, Biological, 01 natural sciences, Mass Spectrometry, Cellulase, polystyrenes, Trypsin, Isoelectric Point, isoelectric point, protein structure, Protein Structure, Quaternary, mass spectrometry, cellulase, cellulase/metabolism, Principal Component Analysis, Proteins, molecular weight, proteins, 0104 chemical sciences, Molecular Weight, trypsin, adsorption, microscopy, Polystyrenes, Adsorption, 0210 nano-technology
Description: The surface immobilization of proteins is an emerging field with applications in a wide range of important areas: biomedical devices, disease diagnosis, biosensing, food processing, biofouling, and bioreactors. Proteins, in Nature, often work synergistically, as in the important enzyme mixture, cellulase. It is necessary to preserve these synergies when utilizing surface immobilized proteins. However, the competitive displacement of earlier adsorbed proteins by other proteins with stronger binding affinities (the "Vroman effect") results in undesired layer instabilities that are difficult to control. Although this nanoscale phenomenon has been extensively studied over the last 40 years, the process through which this competitive exchange occurs is not well understood. This paper uses atomic force microscopy, QCM-D, TOF-SIMS, and in-solution TOF-MS to show that this competitive exchange process can occur through the turning of multilayer protein aggregates. This dynamic process is consistent with earlier postulated "transient complex" models, in which the exchange occurs in three stages: an initial layer adsorbs, another protein layer then embeds itself into the initial layer, forming a "transient complex;" the complex "turns," exposing the first layer to solution; proteins from the first layer desorb resulting in a final adsorbed protein composition that is enriched in proteins from the second layer.
Document Type: Article
Language: English
ISSN: 0927-7765
DOI: 10.1016/j.colsurfb.2012.10.039
Access URL: https://pubmed.ncbi.nlm.nih.gov/23261559
https://research.sabanciuniv.edu/21266/
https://www.sciencedirect.com/science/article/pii/S0927776512005966
https://www.ncbi.nlm.nih.gov/pubmed/23261559
http://www.sciencedirect.com/science/article/pii/S0927776512005966
https://core.ac.uk/display/11743418
https://pubmed.ncbi.nlm.nih.gov/23261559/
https://hdl.handle.net/1959.8/155642
Rights: Elsevier TDM
Accession Number: edsair.doi.dedup.....3689e6142c2000b4b5648718b51ed32d
Database: OpenAIRE
Description
Abstract:The surface immobilization of proteins is an emerging field with applications in a wide range of important areas: biomedical devices, disease diagnosis, biosensing, food processing, biofouling, and bioreactors. Proteins, in Nature, often work synergistically, as in the important enzyme mixture, cellulase. It is necessary to preserve these synergies when utilizing surface immobilized proteins. However, the competitive displacement of earlier adsorbed proteins by other proteins with stronger binding affinities (the "Vroman effect") results in undesired layer instabilities that are difficult to control. Although this nanoscale phenomenon has been extensively studied over the last 40 years, the process through which this competitive exchange occurs is not well understood. This paper uses atomic force microscopy, QCM-D, TOF-SIMS, and in-solution TOF-MS to show that this competitive exchange process can occur through the turning of multilayer protein aggregates. This dynamic process is consistent with earlier postulated "transient complex" models, in which the exchange occurs in three stages: an initial layer adsorbs, another protein layer then embeds itself into the initial layer, forming a "transient complex;" the complex "turns," exposing the first layer to solution; proteins from the first layer desorb resulting in a final adsorbed protein composition that is enriched in proteins from the second layer.
ISSN:09277765
DOI:10.1016/j.colsurfb.2012.10.039