Topic
Vroman effect
About: Vroman effect is a research topic. Over the lifetime, 97 publications have been published within this topic receiving 8841 citations.
Papers published on a yearly basis
Papers
TL;DR: The rates of protein association and dissociation are determined using surface plasmon resonance technology with nanoparticles that are thiol-linked to gold, and through size exclusion chromatography of protein–nanoparticle mixtures, and this method is developed into a systematic methodology to isolate nanoparticle-associated proteins.
Abstract: Due to their small size, nanoparticles have distinct properties compared with the bulk form of the same materials. These properties are rapidly revolutionizing many areas of medicine and technology. Despite the remarkable speed of development of nanoscience, relatively little is known about the interaction of nanoscale objects with living systems. In a biological fluid, proteins associate with nanoparticles, and the amount and presentation of the proteins on the surface of the particles leads to an in vivo response. Proteins compete for the nanoparticle "surface," leading to a protein "corona" that largely defines the biological identity of the particle. Thus, knowledge of rates, affinities, and stoichiometries of protein association with, and dissociation from, nanoparticles is important for understanding the nature of the particle surface seen by the functional machinery of cells. Here we develop approaches to study these parameters and apply them to plasma and simple model systems, albumin and fibrinogen. A series of copolymer nanoparticles are used with variation of size and composition (hydrophobicity). We show that isothermal titration calorimetry is suitable for studying the affinity and stoichiometry of protein binding to nanoparticles. We determine the rates of protein association and dissociation using surface plasmon resonance technology with nanoparticles that are thiol-linked to gold, and through size exclusion chromatography of protein-nanoparticle mixtures. This method is less perturbing than centrifugation, and is developed into a systematic methodology to isolate nanoparticle-associated proteins. The kinetic and equilibrium binding properties depend on protein identity as well as particle surface characteristics and size.
3,085 citations
TL;DR: It is concluded that intact plasma will quickly replace the fibrinogen it has deposited on glass-like surfaces by high molecular weight kininogen and, to a smaller extent, by factor XII.
743 citations
TL;DR: Recording ellipsometers and surface film balance, breath patterns, and ferric oxide powder “staining” were used to observe adsorption of normal plasma constituents onto metal oxide, silicon oxide, and polymer surfaces.
Abstract: Recording ellipsometers and surface film balance, breath patterns, and ferric oxide powder “staining” were used to observe adsorption of normal plasma constituents onto metal oxide, silicon oxide, and polymer surfaces. Adsorbed proteins could be identified by their ability to adsorb matter from corresponding antihuman sera. Data indicate that oxidized silicon crystal surfaces adsorbed fibrinogen out of plasmas within 2 sec; within 20 sec, these films lost their ability to attract antifibrinogen and were later partially removed if intact factor XII was present in the solution. One aminated nonheparinized polymer formed films that adsorbed large amounts of fibrinogen and some gamma globulins out of plasma in the ellipsometer, and platelets out of platelet-rich plasma, as well as ferric oxide out of aqueous suspension. After taking up heparin, these polymer films appeared able to adsorb only small amounts of protein or oxide, and no detectable amounts of fibrinogen or platelets. On another aminated polymer, heparin seemed without effect. Interaction of metal surfaces with plasma may be complicated by oxidation.
431 citations
TL;DR: Recording ellipsometers were used to identify and observe plasma proteins being adsorbed by acid-treated silicon crystal slices (SiW), and by anodized tantalum-sputtered glass slides (TaW), out of blood plasma.
364 citations
TL;DR: 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.
297 citations
Related Topics (5)
Performance Metrics
| Year | Papers |
|---|---|
| 2021 | 4 |
| 2020 | 2 |
| 2019 | 2 |
| 2018 | 4 |
| 2017 | 2 |
| 2016 | 2 |