Ontology highlight
ABSTRACT:
SUBMITTER: Middleton CT
PROVIDER: S-EPMC3334878 | biostudies-literature | 2012 Mar
REPOSITORIES: biostudies-literature
Nature chemistry 20120311 5
Amyloid formation has been implicated in the pathology of over 20 human diseases, but the rational design of amyloid inhibitors is hampered by a lack of structural information about amyloid-inhibitor complexes. We use isotope labelling and two-dimensional infrared spectroscopy to obtain a residue-specific structure for the complex of human amylin (the peptide responsible for islet amyloid formation in type 2 diabetes) with a known inhibitor (rat amylin). Based on its sequence, rat amylin should ...[more]