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Understanding the Interaction of Nanoparticles at the Cellular Interface
Published in D. Sakthi Kumar, Aswathy Ravindran Girija, Bionanotechnology in Cancer, 2023
Any application of nanoparticle in a biological fluid, such as blood, results in the adherence and aggregation of proteins on the surface of NPs; and forms an entirely new entity on the surfaces [33]. This new entity in an in vivo condition is called protein corona (PC) and is divided into two categories: soft and hard corona [35]. Initially, the soft corona is formed when NPs come in contact with biological fluids by the proteins with low-binding affinity. Later on, these loosely bound proteins are replaced with a hard corona composed of less abundant proteins with high-binding affinity [36]. Processing of protein adsorption and corona formation is controlled by a dynamic phenomenon known as the Vroman effect, as provided in Figure 2.3.
Rapid Formation of Plasma Protein Corona Critically Affects Nanoparticle Pathophysiology
Published in Lajos P. Balogh, Nano-Enabled Medical Applications, 2020
Stefan Tenzer, Dominic Docter, Jörg Kuharev, Anna Musyanovych, Verena Fetz, Rouven Hecht, Florian Schlenk, Dagmar Fischer, Klytaimnistra Kiouptsi, Christoph Reinhardt, Katharina Landfester, Hansjörg Schild, Michael Maskos, Shirley K. Knauer, Roland H. Stauber
However, as already evident from the heat maps, which illustrate the kinetic corona protein abundance, we found that the amounts of bound proteins changed significantly over time, that is, quantitatively (Supplementary Figs. S2 and S5–S7). As predicted from the Vroman effect, we observed protein groups that displayed increased or reduced binding over time (Fig. 9.2a, c (protein groups I and II) and Supplementary Fig. S7), which implies that these proteins energetically displace or are displaced by other proteins [28]. Our analysis uncovered novel binding kinetics for biological relevant protein groups for all nanoparticles investigated, which cannot be explained solely by the Vroman effect. Classification of protein-binding modalities unexpectedly identified proteins characterized by low abundance at the beginning of plasma exposure and at later time points, but displaying peak abundance at intermediate time points (Fig. 9.2b, c (protein group III) and Supplementary Fig. S8). Other proteins, however, showed exactly the opposite behaviour, being highly abundant at early and late time points, but not at intermediate time points (Fig. 9.2c (protein group IV) and Supplementary Fig. S8). Previous kinetic studies did not employ quantitative LCMS-based proteomics, and thus these complex binding kinetics went unnoticed until now [7, 14, 16, 29]. Importantly, representative candidates for all binding modalities were verified independently by immunoblot (Fig. 9.2), which underlines the reliability of our analysis. Comparison of the protein-binding groups using Venn diagrams showed no nanoparticle-independent overlap, indicative of particle-specific binding characteristics (Supplementary Figs. S2, S9 and S10). Although the effects of crowding proteins are certainly important [7, 30], the binding patterns observed in a complex physiologically relevant environment cannot be explained by current mathematical corona-evolution models obtained in simplified experimental systems [7, 29–32]. As reviewed by Vogler [33], our knowledge on the regulation of protein binding to nanosized objects in complex environments is, indeed, still limited.
Nonclinical Safety Evaluation of Medical Devices
Published in Pritam S. Sahota, James A. Popp, Jerry F. Hardisty, Chirukandath Gopinath, Page R. Bouchard, Toxicologic Pathology, 2018
Kathleen A. Funk, Victoria A. Hampshire, JoAnn C. L. Schuh
The early response to a medical device occurs after initial injury to the connective tissue and other tissue structures when the device is placed. This is followed by blood clot or thrombus formation and blood protein (albumin, fibrinogen, complement, fibronectin, vitronectin, γ globulin) adsorption onto the surface of the device (Anderson et al. 2008). These innate immune responses involve extrinsic and intrinsic coagulation, complement and platelet activation, fibrinolysis, and elaboration of many bioactive substances such as mitogens, chemoattractants, cytokines/chemokines, and growth factors. This reaction on the device’s surface has been termed the blood-based provisional matrix (Anderson et al. 2008) or the Vroman effect (Hirsh et al. 2013). This effect results in blood proteins with the highest mobility (e.g., fibrinogen) adsorbing to a surface first, but which are then competitively replaced by other proteins that have a higher affinity for the surface. The provisional matrix, partially influenced by the type of device surface, expresses protein ligands that recruit and bind to inflammatory cell integrins at the device site. The biomaterial surface chemistry (Thevenot et al. 2008) and secretions of the host cells also determine the balance of cell adhesion and detachment and cell death at the device surface. For instance, TNF-alpha promotes macrophage apoptosis on biomaterials. The acute cellular reaction is usually several days in duration, exhibits variable involvement of neutrophil and macrophages, and release of secretory components such as histamine from mast cells and cytokine/chemokine release from leukocytes. The subsequent subacute and chronic inflammatory response often consists of a foreign body inflammatory response, which is not an invariable host response at the device-tissue interface. Foreign body responses are typified by variable numbers of granulocytes (PMN or heterophils), mononuclear macrophages that fuse to form multinucleated giant cells, mast cells, plasma cells, and secretory products, including immunoglobulins, complement, cytokines, chemokines, enzymes, growth factors, and peptides (Anderson et al. 2008). Although circulating monocytes were once thought to be the source of infiltrating macrophages in damaged tissues, permanent and specific tissue resident macrophages (e.g., Langerhans cells and dermal macrophages in skin, and resident macrophages in skeletal muscle or adipose tissue), are the likely source of steady-state mononuclear macrophages within lymphoid and nonlymphoid tissues. These tissue resident macrophages readily proliferate in disease states and are involved in activities involving foreign body degradation, phagocytosis, antigen presentation (antibody production and hypersensitivity reactions), fibrosis, and tissue repair. During tissue injury, tissue resident macrophages are supplemented by variable contributions from infiltrating, circulating monocytes that can phenotypically transition to macrophage phenotypes (Davies et al. 2013; Novak et al. 2014).
Nanoparticle-protein corona complex: understanding multiple interactions between environmental factors, corona formation, and biological activity
Published in Nanotoxicology, 2021
Aysel Tomak, Selin Cesmeli, Bercem D. Hanoglu, David Winkler, Ceyda Oksel Karakus
Clearly, a complete description of the NP-protein corona complex involves the characterization of the composition and concentration of the adsorbed proteins and their conformation on the surface of NPs over time. In the past decade, substantial progress has been made in understanding the interactions of NPs with proteins under physiological conditions and in characterizing the suite of proteins bound to the NP surface resulting from these interactions (Cedervall et al. 2007; Lundqvist et al. 2011; Del Pino et al. 2014). The literature indicates that spectroscopic and gel-electrophoresis techniques are well-suited for the identification of proteins adsorbed on NP surfaces (Carrillo-Carrion, Carril, and Parak 2017; Pederzoli et al. 2017). However, the structure of the protein adsorption layer changes with environment and time, as described by the Vroman effect (Vroman 1962), making the characterization difficult and the comparison of findings across studies challenging. Table 2 lists the analytical methods commonly used to study different aspects of NP-protein corona formation, together with advantages and disadvantages of each technique.
Proteome analysis of the salivary pellicle formed on titanium alloys containing niobium and zirconium
Published in Biofouling, 2019
Heloisa Navarro Pantaroto, Karina Pintaudi Amorim, Jairo Matozinho Cordeiro, João Gabriel S. Souza, Antônio Pedro Ricomini-Filho, Elidiane C. Rangel, Ana Lúcia R. Ribeiro, Luís Geraldo Vaz, Valentim A.R. Barão
Despite the fact that the surface properties of the Ti materials (ie roughness) had an important effect on protein adsorption (Dodo et al. 2013), the physical properties of the materials tested here did not appear to affect the protein–material interaction, as the Ti materials studied showed similar surface properties (roughness and wettability) but differences in salivary pellicle composition. Reports in the literature have shown that changes in the chemical composition of the Ti surface are able to change the proteomic profile of the salivary pellicle formed (Oughlis et al. 2011; Romero-Gavilán et al. 2017). Indeed, different biomaterials, in terms of composition, can change proteomic profiles adsorbed on surfaces and, consequently, the interaction with epithelial cells (Abdallah et al. 2017). Therefore, it is expected that the chemical composition of Ti materials may be the driving force toward surface and salivary protein interactions (Cavalcanti et al. 2014). Protein adsorption on the surface is mediated by non-covalent interactions, such as ionic bonding (Nakanishi et al. 2001). Moreover, the Vroman effect is expected in this process, which describes the competitive adsorption on solid surfaces; in this case, proteins with a higher affinity for surfaces and adsorbing slowly can adsorb on surfaces, replacing smaller proteins with high diffusion and rapid adsorption (first proteins adsorbed), but low surface affinity (Rabe et al. 2011).
In Vitro models for thrombogenicity testing of blood-recirculating medical devices
Published in Expert Review of Medical Devices, 2019
Within seconds of blood exposure, biomaterial surfaces rapidly adsorb serum proteins onto their surface. These proteins desorb and are exchanged for higher binding affinity proteins in a process known as the Vroman Effect. Figure 1 illustrates the pro-thrombotic events catalyzed by biomaterial contact and the Vroman pattern: albumin, immunoglobulin G (IgG), fibrinogen, and high molecular weight kininogen (HMWK) [15]. Platelets interacting with these bound proteins adhere to the material and upregulate membrane-bound phosphatidylserine [16]. The downstream pro-thrombotic processes from platelet activation are illustrated in Figure 2. When serum proenzymes such as prothrombin bind at this active site, zymogen-protease conversions produce the active form of the enzyme, thrombin [17–19]. In platelet aggregates, thrombin amplifies the coagulation response. A positive feedback loop is created that increases platelet activation through platelet activation factor (PAF), proteinase-activated receptor (PAR) 1 and 4 on platelet membranes [20]. Platelets also degranulate, releasing cytokines [21] and develop pseudopodia to strengthen adherence to the surface and other platelets [22]. Thromboxane A2 diffuses across the platelet plasma membrane and acts as an activator for other platelets [23]. Under flow conditions, platelets are captured through interaction with von Willebrand factor (vWF). This interaction is mediated through two receptors: GPIb-IX-V and platelet integrin (αIIbβ3). Active thrombin cleaves at least two sites on the fibrinogen molecule making non-covalent interactions between fibrinogen molecules [24,25] producing aggregated insoluble fibrin fibers. The fibers are crosslinked by Factor XIII [26] to form an aggregated structure that can trap platelets, red blood cells, and thrombin by binding at two distinct binding sites [20]. The fibrin-mediated clot is susceptible to fibrinolysis via plasmin, an enzyme protease [24].