Journal
CHEMICAL COMMUNICATIONS
Volume 52, Issue 38, Pages 6391-6394Publisher
ROYAL SOC CHEMISTRY
DOI: 10.1039/c6cc01248e
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Funding
- NIH [GM094693]
- American Diabetes Association
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM094693] Funding Source: NIH RePORTER
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An oligoquinoline foldamer library was synthesized and screened for antagonism of lipid bilayer catalysed assembly of islet amyloid polypeptide (IAPP). One tetraquinoline, ADM-116, showed exceptional potency not only in this assay, but also in secondary assays measuring lipid bilayer integrity and rescue of insulin secreting cells from the toxic effects of IAPP. Structure activity studies identified three additional oligoquinolines, closely related to ADM-116, which also have strong activity in the primary, but not the secondary assays. This contrasts work using an oligopyrdyl foldamer scaffold in which all three assays are observed to be correlated. The results suggest that while there is commonality to the structures and pathways of IAPP conformational change, it is nevertheless possible to leverage foldamers to separately affect IAPP's alternative gains-of-function.
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