The Inhibition Pathways of Human Islet Amyloid Polypeptide
Poster Oct 15, 2019
Yuko P. Y. Lam; Cookson K.C. Chiu; Christopher A. Wootton; Ji-Inn Song; Meng Li; Ian Hands-Portman; Mark P. Barrow and Peter B. O'Connor.
Amyloid proteins are inherently disordered molecules, with a highly flexible conformation; as a result, they are prone to forming aggregates, which have been linked to a variety of diseases. As a result of their disorder, classic structure-based design for therapeutics against amyloid proteins is challenging.
Download this poster to find out more about:
- Human islet amyloid polypeptide (hIAPP).
- How mass spectrometry can be used to identify how hIAPP inhibitors work.
- The inhibitors most successful at preventing hIAPP aggregation.
The changing landscape for antibody-derived therapeutics, such as bi-specific monoclonal antibodies, Fab fragments and Fc-fusion proteins brings new purification challenges in the downstream processing of these molecules. Standard chromatography resins, such as Protein A, may not result in the most efficient purification process.READ MORE