Abstract
We utilized solution-phase biopanning to obtain a de novo peptide (LA12) that specifically bound to the core region of the human amylin monomer. LA12 stabilized the random coil conformation of amylin to suppress aggregation in a dose-dependent manner with the highest suppression effect of 78% and reduced the cytotoxicity of amylin.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 1633-1636 |
| Number of pages | 4 |
| Journal | Chemical Communications |
| Volume | 56 |
| Issue number | 11 |
| DOIs | |
| State | Published - 2020 |
Bibliographical note
Funding Information:This work was sponsored by the Natural Science Foundation of Shanghai (19ZR1412400), CAMS Innovation Fund for Medical Sciences (CIFMS 2018-I2M-3-006), the Fundamental Research Funds for the Central Universities (2018PT31028), the Open Project Fund provided by Key Laboratory for Biomedical Effects of Nanomaterials and Nanosafety, CAS (NSKF201812), and the National Natural Science Foundation of China (21636003 and 31901007).
Publisher Copyright:
This journal is © The Royal Society of Chemistry.
