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Phototherapy Using Nanomaterials
Published in D. Sakthi Kumar, Aswathy Ravindran Girija, Bionanotechnology in Cancer, 2023
A. N. Resmi, V. Nair Resmi, C. R. Rekha, V. Nair Lakshmi, Shaiju S. Nazeer, Ramapurath S. Jayasree
Albumin is a plasma protein, which is responsible for blood colloidal osmotic pressure. This is non-antigenic and biodegradable and has been studied extensively as a drug carrier. The average HSA half-life is 19 days [177]. The photosensitizer pheophorbide was loaded on human serum albumin (Pheo-HSA) nanoparticles with different cross-linked ratios by non-covalent adsorption. Intracellular uptake and phototoxicity of both pheophorbide and Pheo-HSA nanoparticles were studied in Jurkat cells. For irradiation, a laser diode with emission at 668 nm and a light dose of 96 mJ/cm2 were used as light source. Due to intramolecular interactions, 1O2 quantum yield of pheophorbide-loaded HSA nanoparticles was very low and the final phototoxicity was at the same level as induced by free pheophorbide [178].
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].
Applications of Green Polymeric Nanocomposites
Published in Satya Eswari Jujjavarapu, Krishna Mohan Poluri, Green Polymeric Nanocomposites, 2020
Mukesh Kumar Meher, Krishna Mohan Poluri
Serum albumin exists as a globular blood protein having an approximate molecular weight of 65 kDa. It is found in the blood of vertebrates, being especially abundant in mammal blood (Moman and Varacallo 2018). It consists of 585 amino acids which form three repetitive homologous domains and these are separated by two sub-domains in their globular structure. The most essential role of albumin is to maintain oncotic pressure in blood which is needed for proper body fluid distribution. Human and bovine serum albumins are the most studied albumins due to their obvious importance in metabolic, genetic and in vitro/in vivo clinical studies (Peters Jr 1985). Albumins are moderately soluble (up to 40% w/v) at physiological pH and perform as an excellent natural carrier for metabolic products such as steroid hormones, hemins, fatty acids, bilirubin, thyroxine and various drugs (van der Vusse 2009, Zilg et al. 1980). Albumin shows high stability in wide pH ranges from 4 to 9 and temperature up to 60°C for 10 hours of heating without any degradation/aggregation. Biodegradability and a high stability structure enable albumins to be employed as appropriate drug nano-carriers, and for encapsulating polymers in biomedical applications (Rai et al. 2017).
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.
Significant biopolymers and their applications in buccal mediated drug delivery
Published in Journal of Biomaterials Science, Polymer Edition, 2021
Albumin is the main plasma protein found in human blood. Albumin is stable over a wide range of pH from 4-9 and in temperature <60 °C. It has various advantageous properties such as biodegradability, low toxicity, immunogenicity, and most importantly it is suitable for blood circulation (half period 19 days). These properties make it a suitable drug carrier. Albumin has an effective binding capacity for multiple drugs due to the presence of multiple drug binding sites. Human serum albumin (HSA) is used to transport several therapeutic drugs. It is a suitable agent for gene therapy as it does not interact with the serum [18]. Albumin can be obtained from a variety of sources such as ovalbumin, BSA (bovine serum albumin), and HSA. Albumin is highly soluble 40% w/v at 7.4 pH which makes it the best material for drug delivery. It is widely used as nanoparticles and nanospheres for drug delivery [20].
Evaluation of models for predicting pediatric fraction unbound in plasma for human health risk assessment
Published in Journal of Toxicology and Environmental Health, Part A, 2021
Yejin Esther Yun, Andrea N. Edginton
In order to instill confidence in PBPK model outputs, an accurate determination of the fraction unbound in plasma (fup) is essential and has been identified as one of the most important inputs driving pediatric PBPK model outputs (Yun and Edginton 2019). Among the 60 plasma proteins in humans, albumin, alpha acid glycoprotein (AAG), and lipoproteins meaningfully bind to exogenous compounds (Burton et al. 2006; Notarianni 1990). While acid-base properties of a compound generally determine which plasma protein it preferentially binds this assumption is not always valid. Neutral and acidic compounds tend to bind to albumin, while basic compounds tend to bind to AAG and lipoproteins (Burton et al. 2006). The physiological roles of these plasma proteins are manifold, in that these constituents serve as both a transporter and a storage depot for endogenous and exogenous substances (Lehman-McKeeman 2010). Albumin maintains the osmotic pressure in the bloodstream and transports endogenous molecules such as bilirubin and fatty acids (Putnam 1975). AAG is an acute-phase reactant; when presented with injury and inflammation, plasma AAG levels increase (Israili and Dayton 2001). Decreased AAG levels are associated with severe liver diseases including cirrhosis (Barre et al. 1984; Israili and Dayton 2001)). AAG serves as a carrier of exogenous substances. Lipoproteins transport lipid molecules or lipid-soluble compounds (Lemaire et al. 1986).