Thermal unfolding of human lysozyme induces aggregation: Recognition of the aggregates by antisera against the native protein

October 11, 2018

Title

Thermal unfolding of human lysozyme induces aggregation: Recognition of the aggregates by antisera against the native protein

Author

Md. Tauqir Alam, Asim Rizvi, Mohd. Ahmar Rauf, Mohammad Owais, Aabgeena Naeem

Year

2018

Journal

International Journal of Biological Macromolecules

Abstract

Protein aggregates are formed due to the inappropriate folding of polypeptides. Human lysozyme (HLZ) plays an important role in the innate immune response of the body and has been used extensively as a model protein to study aggregation. In this study, we showed that HLZ undergoes unfolding induced aggregation when heated. We further showed that the aggregates were recognized by polyclonal antibodies against the native HLZ. The consequences of these observations are further co-related with mammalian physiology.

Instrument

J-815

Keywords

Circular dichroism, Secondary structure, Thermal stability, Aggregation, Biochemistry