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Freeze-Drying: Principles and Practice
Published in Sandeep Nema, John D. Ludwig, Parenteral Medications, 2019
Steven L. Nail, Larry A. Gatlin
Amorphous excipients include disaccharides such as sucrose, trehalose, and occasionally, lactose or maltose. These excipients may play a double role in a formulation as both a bulking agent and, for proteins and other biologicals, as a stabilizer. In order to be effective, the stabilizer must be amorphous and remain so throughout the shelf life of the product. Human serum albumin is used in several protein formulations as both a stabilizer of the protein in the solid state and also as a competitive surfactant to inhibit loss of the active protein by adsorption to surfaces such as plastic tubing, filters, or gaskets. A detailed discussion of mechanisms of stabilization of biological formulations is outside the scope of this chapter, and the reader is referred to publications by Carpenter et al. (4), Arakawa et al. (5), Cleland et al. (6), and Chang et al. (7).
Prenatal and postnatal transfer of perfluoroalkyl substances from mothers to their offspring
Published in Critical Reviews in Environmental Science and Technology, 2022
Yingxue Liu, An Li, Qi An, Kai Liu, Ping Zheng, Shanshan Yin, Weiping Liu
Human serum albumin (HSA) is a predominant protein in human blood and critically important in the transfer of various compounds. It has been reported that the PFAS-protein complexes could prevent PFASs from passing through the placenta, while free PFASs in blood were able to cross the barrier (Pan et al., 2017). In order to explore the transplacental transfer mechanism of chiral 1 m-PFOS, Zhao et al. determined the affinities between HSA and 1 m-PFOS enantiomers by using an in silico molecular docking simulation. The results of the simulation showed that the interaction between HSA and two 1 m-PFOS enantiomers was enantioselective. Therefore, the enantioselective carrier protein affinity might be a key influencing factor for stereoselective transplacental transfer of 1 m-PFOS (Zhao et al., 2020).
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].
Binding affinity studies of 1,2,3-triazole copper(II) complexes to human serum albumin
Published in Journal of Coordination Chemistry, 2018
Queite A. de Paula, Jean-Pierre Joly, Katalin Selmeczi, David E. P. Fonseca, Giovanni F. Caramori, Nicholas P. Farrell, Ana M. Da Costa Ferreira
Human serum albumin is a protein which functions as a plasma carrier, a transporter protein, and as an essential molecule for maintaining osmotic pressure in body tissues. Structural changes in HSA may be caused by the approach of endogenous or exogenous binders, including fatty acids, hormones, toxic metabolites, and several drugs with moderate affinity (Ka = 104 to 106 M−1) [60, 61]. Therefore, modifications in the HSA by a substrate can be associated with its binding affinity and capacity of promoting degradation or oxidation, and could influence the pharmacokinetics of several drugs, affecting their distribution in a specific target as well as their rates of metabolism and excretion. To calculate the relative stability constants KCuL for each triazole ligand, a copper-aqua complex ([Cu(H2O)4]SO4·H2O) was used as a control, and the stoichiometric relations were considered, as described elsewhere [51],