Analysis of Protein Aggregates Conformational Changes & Folding State by Fluorescence Spectroscopy (CAT#: STEM-B-0307-CJ)

Introduction

The generic term 'aggregates' refers to species characterized by a wide size range, diverse morphologies and structures. Protein aggregates may start in the low nanometer size range but then can grow into the micrometer and even visible size range.

Most protein therapeutics and many other biopharmaceutical compounds are inherently unstable and can undergo aggregation through various pathways. Aggregates of various kinds can be formed, such as reversible and non-reversible, soluble, and non-soluble etc. In addition,Aggregation maybe occur because of exposure to air-liquid or liquid-solid interfaces, e.g., during mixing, during filling and shipping, during reconstitution of lyophilized products, or through contact with chromatography columns, pumps, pipes, vessels, filters, etc. Aggregation can directly influence the efficacy of the therapy by reducing the number of functional molecules, but also indirectly influence efficacy as well as safety of a therapy by inducing side-effects, such as unwanted immunogenicity.

In biochemistry, a conformational change is a change in the shape of a macromolecule, often induced by environmental factors. Protein folding is the physical process by which a protein chain is translated into its native three-dimensional structure, typically a "folded" conformation, by which the protein becomes biologically functional.