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The Use of Capillaroscopy and Aggregometry Methods to Diagnose the Alterations of Microcirculation and Microrheology in Diabetes
Published in Andrey V. Dunaev, Valery V. Tuchin, Biomedical Photonics for Diabetes Research, 2023
Andrei E. Lugovtsov, Yury I. Gurfinkel, Petr B. Ermolinskiy, Anastasia A. Fabrichnova, Alexander V. Priezzhev
RBCs interact with each other forming linear or more complex structures (i.e., RBC aggregates (Figure 3.1)) under low shear rates. These structures can be reversibly dispersed into singe cells under high shear rates. Normally, RBCs are in dynamic equilibrium, constantly aggregating and disaggregating in vivo [26]. It is crucial to note that RBC aggregation occurs only in solutions with macromolecules of high molecular weight. In the case of blood plasma, they are fibrinogen, albumin, etc. [26].
Development and Application of Phase Change Materials in the Biomedical Industry
Published in Atul Sharma, Amritanshu Shukla, Renu Singh, Low Carbon Energy Supply Technologies and Systems, 2020
Abhishek Anand, Amritanshu Shukla, Atul Sharma
It is the liquid part of the blood. The RBCs, WBCs, and platelets remain suspended in plasma. Plasma contains mostly water and dissolved proteins, glucose, electrolytes, hormones, O2, CO2, etc. Blood plasma is separated from the whole blood through centrifugation where the blood cells are settled at the bottom of the centrifugation tube and plasma is collected at the top. The plasma is then separated. The blood from which plasma is separated within 24 hours of collection is at a temperature below −25oC. It has a storage life of 3 years when stored at this temperature. It can be also stored between the temperature range of −18oC to −25oC but with a reduced shelf life of 3 years.
Nanoparticles in Cancer Treatment: Types and Preparation Methods
Published in Hala Gali-Muhtasib, Racha Chouaib, Nanoparticle Drug Delivery Systems for Cancer Treatment, 2020
Jyoti Ahlawat, Emmanuel Zubia, Mahesh Narayan
Polypeptide-based nanoparticles present a unique advantage over other nanoparticles in regards to toxicity and unique functionalities that depend on the chemical composition of the protein and their surface scaffolds. Endogenous proteins are often used for the creation of nanoparticles as they elicit a low immune response, and some of their physicochemical properties (biodegradability, nonantigenicity, metabolism, surface charge, and structure) are already well defined. If the protein reagents are pure, these nanoparticles are relatively easy to prepare. One of the most ubiquitously used proteins in nanoparticle research is albumin. Albumin is a globular protein found in blood plasma and functions as a transporter of fatty acids, hormones and other compounds. In the context of nanoparticles, this protein makes use of its hydrophobic motif to reversibly bind hydrophobic chemotherapeutics and increase their bioavailability. One of the advantages of albumin is that it binds to glycoprotein 60, which mediates transcytosis, allowing it to be transported to the interior of the cell [13]. Figure 2.2A provides an illustration of a single monomeric protein assembled into a nanoparticle with a hollow cavity. An example of an albumin bound nanoparticle is Abraxane® (Celgene). This paclitaxel–albumin-bound nanoparticle increases the solubility and tumor delivery of paclitaxel, a drug that was approved by the FDA to treat breast cancer [12].
Physicochemical and biological properties of nanohydroxyapatite grafted with star-shaped poly(ε-caprolactone)
Published in Journal of Biomaterials Science, Polymer Edition, 2022
Eleni Cristina Kairalla, José Carlos Bressiani, Ana Helena de Almeida Bressiani, Maria Tereza de Carvalho Pinto Ribela, Olga Zazuco Higa, Alvaro Antonio Alencar de Queiroz
HAP coatings are generally considered to improve the osseointegration of biomedical implants. It is generally assumed that selective adsorption of plasma proteins to the implant surface material is a critical factor for cellular activation pathways. Several of these proteins are present in blood plasma such as albumin (HSA), von Willebrand factor, fibrinogen (HFb), and fibronectin. Even after a very short exposure time, these proteins bind to the synthetic surfaces that will influence further interactions with integrins and cellular activation pathways. It has previously been shown that a model system of fibrinogen and the major platelet membrane receptor (GPIIb-IIIa) can be used to predict the performance of the hemocompatibility of biomaterials [53]. The study of HSA and HFb adsorptions onto SPCL-g-HAPN will contribute to elucidating the mechanisms involved in the biocompatibility of the nanocomposite SPCL-g-HAPN.
Using fluorescence and circular dichroism (CD) spectroscopy to investigate the interaction between di-n-butyl phthalate and bovine serum albumin
Published in Journal of Environmental Science and Health, Part A, 2022
Serum albumin, the most abundant protein constituent in blood plasma, plays a fundamental role in the disposition and transportation of various molecules and can react with many different ligands in vivo and in vitro.[12,13] As the biological functions of a protein depend on its structure, the resultant structural alternations due to its interaction with ligands can affect the transport, metabolism, and availability of serum albumin for other ligands.[13,14] Normally, pollutants will interact with serum albumin after they enter the bloodstream. Bovine serum albumin (BSA) was used as the model protein because of its water-solubility, its stability, as well as its sequence similarity to human serum albumin (HSA)[15] for evaluating the di-n-butyl phthalate toxicity to health.
Technetium-99m metastable radiochemistry for pharmaceutical applications: old chemistry for new products
Published in Journal of Coordination Chemistry, 2019
Bianca Costa, Derya Ilem-Özdemir, Ralph Santos-Oliveira
Both body fluids and cell culture media are complicated because of their heterogeneity. For example, blood plasma contains fat particles, called lipoproteins responsible for the transport of triglycerides, phospholipids and cholesterol in plasma; large proteins (such as immunoglobulins, albumin and transferrin); as well as many small molecules and ions. In this medium, the compounds can be chemically transformed by in vivo chemical reactions, which are the main sources of radiation toxicity, which may result in a change in the pharmacokinetics of the radiopharmaceutical [7, 88].