Advanced Structure: High Order Structure

Unlike small molecule drugs, biologics is generated in the system of life.They not only have primary structure, and the secondary and tertiary structure, quaternary structure may even exist.To determine the biological drugs advanced structure to ensure its efficacy, stability and safety are very important.

Nuclear magnetic resonance (NMR) technology is the ideal choice for protein structure analysis, can be in the process of r&d and production of biological treatment, identify whether it is a key structural changes.Because of its structure itself can provide abundant information, so the NMR in senior protein structure plays a unique role.Biological detection methods for the treatment of drug and therefore more streamlined.With the development of data acquisition and analysis technology, is now available in physiological conditions, the related research has the natural abundance of complete protein molecules (including monoclonal antibody).A brand newMbioHOSSoftware can provide a set of two kinds of measurement methods, used to determine the advanced structure of biological treatment.Now, for biosimilars and the similarity between its standard assessment is also becoming more and more simple, fast detection can be quickly determined whether qualified pharmaceuticals.

FT - IR was used to resolve one of the orthogonal test method of advanced structure, it is mainly used for analysis of protein secondary structure.FT - IR detection is not only time-consuming short (about 1 minute/samples), properties of different samples required is extremely loose (e.g., protein concentration, buffer composition and excipients, etc.).These qualities make FT - IR, became the biopharmaceutical development phase for the best means for the monitoring of the protein conformations, and it can also be used in routine quality control.

Right example shows a antibody at different temperature (25-95 ° C) of the infrared spectrum.60 ° C, amide I take shape, there is no change, protein folding structure can maintain its natural.Further heat led to the decrease of the amide I band strength, it shows that the intramolecular beta fold.