AI Article Synopsis
- Conformationally-constrained molecules can target protein surfaces, potentially influencing how proteins fold, which is important given the link between protein misfolding and various diseases.
- The study introduces a new class of non-peptidic scaffolds that utilize S···O interactions to resemble critical features of protein surfaces.
- These novel molecules demonstrate the ability to prevent the fibrillation of islet amyloid polypeptide (IAPP), which is associated with type II diabetes pathology.
Article Abstract
Conformationally-constrained molecules that selectively recognise the surfaces of proteins have the potential to direct the path of protein folding. Such molecules are of therapeutic interest because the misfolding of proteins, especially that which results in fibrillation and aggregation, is strongly correlated with numerous diseases. Here we report the novel use of S···O interactions as a conformational control element in a new class of non-peptidic scaffold that mimics key elements of protein surfaces. These molecules disrupt the fibrillation of islet amyloid polypeptide (IAPP), a process that is implicated in the pathology of type II diabetes.
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Source |
|---|---|
| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC5363787 | PMC |
| http://dx.doi.org/10.1039/c6sc00756b | DOI Listing |
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