Programme

P.77 -- Posters, VCTP-51

Date: Thursday, 6 August 2026

Time: 09:30 - 10:30

Structures and Dynamics of α-Synuclein in Different States: A Molecular Dynamics Study

Tran Thi Minh Thu1,2*, Pham Phi Dung1,2, Tran Thi Hanh2,3, Nguyen Truong Co4, Nguyen Hoang Linh5 and Mai Suan Li6

1Faculty of Materials Science and Technology, Ho Chi Minh City University of Science-VNUHCM, 227 Nguyen Van Cu Street, District 5, Ho Chi Minh City, Viet Nam 2Vietnam National University, Ho Chi Minh City 700000, Vietnam 3Faculty of Physics and Engineering Physics, Ho Chi Minh City University of Science -VNUHCM, 227 Nguyen Van Cu Street, District 5, Ho Chi Minh City, Viet Nam 4Institute of Fundamental Technological Research, PAN, Poland 5Duy Tan University, Viet Nam 6Institute of Physics, Polish Academy of Sciences, Al. Lotników 32/46, 02-668 Warsaw, Poland

Parkinson’s disease (PD) is a slowly progressive movement disorder resulting from the loss of dopaminergic neurons in the substantia nigra, a small area of cells in the mid-brain. Both genetic and environmental factors play a huge role in causing this illness. Several evidence link α-synuclein (α-Syn), a small highly conserved presynaptic protein with unknown function, to both familial and sporadic PD. In fact, rare familial cases of PD are associated with missense point mutation in α-Synuclein, or with overexpression of the wild-type protein due to its gene duplication both in vivo and in vitro and are associated with accelerated progression of PD. Experimental studies have shown that C-terminal truncation stabilizes the fibrillar state of α-Syn, whereas graphene-based nanomaterials can modulate or even inhibit its aggregation. In this work, we employed all-atom replica-exchange and conventional molecular dynamics simulations to investigate α-Syn in multiple structural and oligomeric states, including truncated and full-length forms. Furthermore, coarse-grained molecular dynamics was used to characterize the oligomerization pathway, enabling us to track oligomer lifetimes and intermediate species relevant to early aggregation. Together, these simulations provide a comprehensive view of how structural variants and nanoscale environments influence the conformational landscape and aggregation propensity of α-Syn.

Presenter: Tran Thi Minh Thu