Charged Tubular Supramolecule Boosting Multivalent Interactions for the Drastic Suppression of Aβ Fibrillation

التفاصيل البيبلوغرافية
العنوان: Charged Tubular Supramolecule Boosting Multivalent Interactions for the Drastic Suppression of Aβ Fibrillation
المؤلفون: Jun-Li Hou, Zhao-Jun Yan, Lehui Xiao, Shijing Yue, Chenhong Zhang, Zhongju Ye
المصدر: Nano Letters. 21:10494-10500
بيانات النشر: American Chemical Society (ACS), 2021.
سنة النشر: 2021
مصطلحات موضوعية: Fibrillation, chemistry.chemical_classification, Amyloid, Amyloid beta-Peptides, Chemistry, Mechanical Engineering, Pillar, Supramolecular chemistry, Bioengineering, Peptide, General Chemistry, Condensed Matter Physics, Fibril, Peptide Fragments, nervous system diseases, Alzheimer Disease, Molar ratio, Biophysics, medicine, Humans, General Materials Science, medicine.symptom
الوصف: Anti-Aβ therapy has dominated clinical trials for the prevention and treatment of Alzheimer's disease (AD). However, suppressing Aβ aggregation and disintegrating mature fibrils simultaneously remains a great challenge. In this work, we developed a new strategy using a charged tubular supramolecule (CTS) with pillar[5]arene as the backbone and modifying amino and carboxyl groups at the tubular terminals (noted as CTS-A, CTS-A/C, and CTS-C, respectively) to suppress Aβ fibrillation for the first time. According to the spectroscopic and microscopic characterizations, Aβ40 fibrillation can be efficiently suppressed by CTS-A in a very low inhibitor:peptide (I:P) molar ratio (1:10). A greatly alleviated cytotoxic effect of Aβ peptides after the inhibition or disaggregation process is further disclosed. The well-organized supramolecular structure drives multivalent interaction and gains enhanced efficiency on amyloid fibrillar modulation. These results open a new path for the design of supramolecules in the application of AD treatment.
تدمد: 1530-6992
1530-6984
URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dfb54914131cf865dc310eab02249ced
https://doi.org/10.1021/acs.nanolett.1c04007
حقوق: CLOSED
رقم الأكسشن: edsair.doi.dedup.....dfb54914131cf865dc310eab02249ced
قاعدة البيانات: OpenAIRE