Protein aggregation dealing with

The chapter has dealt with the stability and stabilisation of colloidal systems and covered topics such as their formation and aggregation. If the particle size of a colloidal particle determines its properties (such as viscosity or fate in the body), then maintenance of that particle size throughout the lifetime of the product is important. The emphasis in the section on stability is understandable. Various forms of emulsions, microemulsions and multiple emulsions have also been discussed, while other chapters deal with other important colloidal systems, such as protein and polymer micro- and nanospheres and phospholipid and surfactant vesicles. 

There have been quite a few papers published which deal with fluorescence methods in prion research. Generally, three different approaches have been utilized. First, PrP chimeras with fluorescent proteins (e.g., green fluorescent protein, GFP) have been produced to study various aspects of cellular questions or protein folding. For example, fluorescence imaging techniques have been applied to study prion propagation in yeast (reviewed in [45]). Other examples concern attempts to study protein folding and the nature of aggregates. Kawei-Noma et al. analyzed the... 

In this section, the folding and the presently known conformational states of disufide-intact recombinant prion proteins are discussed. Section 111 deals with biophysical studies on folding and aggregation of reduced... 

The term structure, as used in chemistry and biology, relates both to molecules and to molecular aggregates. A simple example is provided by water. We can deal with the structure of the H2O molecules and also with the way in which these molecules are associated in solid ice and in liquid water. A more complicated example is a biological membrane, where we face the problem of the molecular structures of protein, lipid, and other molecules, and also of the way these molecules are aggregated in the membrane. In this chapter we are concerned with both of these problems, but more attention is given to the structures of individual molecules. We deal with some of the experimental methods used for investigating structure and with some of the structural information which has been accumulated. 

This chapter deals with a specific test of blood-surface interaction in vitro platelet retention in a column of beads (due to platelet adhesion and aggregation). Protein adsorption precedes platelet adsorption, and thus the in vitro platelet retention test involves competitive and sequential adsorption of proteins, the outcome of which produces surfaces having widely varying degrees of platelet retention. Except in the case of thrombin (3), plasma protein absorption on these surfaces has not been studied. 

For solid dosage forms, scale-up is a major challenge and includes ensuring the bioequivalency of the clinical product to the commercial product. For proteins, shear-induced aggregation can be an issue, as well as establishment of a commercial supply chain that is robust, reliable, and able to deal with large amounts of temperature-controlled materials. 

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