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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.