Site-specific chirality-conferred structural compaction differentially mediates the cytotoxicity of Aβ42

Author:

Li Gongyu12ORCID,Jeon Chae Kyung3,Ma Min4,Jia Yifei1,Zheng Zhen5,Delafield Daniel G.4ORCID,Lu Gaoyuan4ORCID,Romanova Elena V.6,Sweedler Jonathan V.6ORCID,Ruotolo Brandon T.3ORCID,Li Lingjun4ORCID

Affiliation:

1. State Key Laboratory of Pharmaceutical Chemical Biology, Research Center for Analytical Science and Tianjin Key Laboratory of Biosensing and Molecular Recognition, Frontiers Science Center for New Organic Matter, College of Chemistry, Nankai University, Tianjin 300071, China

2. Haihe Laboratory of Sustainable Chemical Transformations, Tianjin 300192, China

3. Department of Chemistry, University of Michigan, Ann Arbor, MI 48109, USA

4. School of Pharmacy and Department of Chemistry, University of Wisconsin–Madison, 777 Highland Ave., Madison, WI 53705, USA

5. School of Pharmacy, Tianjin Medical University, Tianjin 300070, China

6. Department of Chemistry and The Beckman Institute for Advanced Science and Technology, University of Illinois at Urbana–Champaign, Urbana, Illinois 61801, USA

Abstract

Analytical and technological advancements in multidimensional ion mobility-mass spectrometry and molecular dynamic simulations catalyze the birth of a new precise strategy for fine-tuning Aβ42 structure and cytotoxicity.

Funder

National Key Research and Development Program of China

National Natural Science Foundation of China

National Science Foundation

Fundamental Research Funds for the Central Universities

Nankai University

National Institutes of Health

Wisconsin Alumni Research Foundation

Division of Molecular and Cellular Biosciences

Publisher

Royal Society of Chemistry (RSC)

Subject

General Chemistry

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