The Inhibition Pathways of Human Islet Amyloid Polypeptide
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.
