| Title | Aromatic-interaction-mediated inhibition of -amyloid assembly structures and cytotoxicity |
| Authors | Xie, Hanyi Peng, Jiaxi Liu, Changliang Fang, Xiaocui Duan, Hongyang Zou, Yimin Yang, Yanlian Wang, Chen |
| Affiliation | Natl Ctr Nanosci & Technol, CAS Key Lab Standardizat & Measurement Nanotechno, CAS Key Lab Biol Effects Nanomat & Nanosafety, CAS Ctr Excellence Nanosci,CAS Ctr Excellence Bra, Beijing 100190, Peoples R China. Peking Univ, Acad Adv Interdisciplinary Studies, Beijing 100871, Peoples R China. |
| Keywords | abeta aggregation inhibition aromatic-interaction SHEET-BREAKER PEPTIDE ALZHEIMERS-DISEASE FIBRIL FORMATION BETA-PEPTIDE PROTEIN AGGREGATION TOXICITY KLVFF NANOPARTICLES DESIGN OLIGOMERS |
| Issue Date | 2017 |
| Publisher | JOURNAL OF PEPTIDE SCIENCE |
| Citation | JOURNAL OF PEPTIDE SCIENCE.2017,23(9),679-684. |
| Abstract | Abnormal aggregation of -amyloid (A) peptide plays an important role in the onset and progress of Alzheimer's disease (AD); hence, targeting A aggregation is considered as an effective therapeutic strategy. Here, we studied the aromatic-interaction-mediated inhibitory effect of oligomeric polypeptides (K8Y8, K4Y8, K8W8) on A42 fibrillization process. The polypeptides containing lysine as well as representative aromatic amino acids of tryptophan or tyrosine were found to greatly suppress the aggregation as evaluated by thioflavin T assay. Circular dichroism spectra showed that the -sheet formation of A42 peptides decreased with the polypeptide additives. Molecular docking studies revealed that the oligomeric polypeptides could preferentially bind to A42 through - stacking between aromatic amino acids and Phe19, together with hydrogen bonding. The cell viability assay confirmed that the toxicity of A42 to SH-SY5Y cells was markedly reduced in the presence of polypeptides. This study could be beneficial for developing peptide-based inhibitory agents for amyloidoses. Copyright (c) 2017 European Peptide Society and John Wiley & Sons, Ltd. |
| URI | http://hdl.handle.net/20.500.11897/471266 |
| ISSN | 1075-2617 |
| DOI | 10.1002/psc.3011 |
| Indexed | SCI(E) |
| Appears in Collections: | 前沿交叉学科研究院 |
