Our Mission

SynuSight is dedicated to pioneering innovations in neurodegenerative diseases through cutting-edge, interdisciplinary technologies, delivering transformative diagnostics and therapeutics to benefit millions of patients worldwide.

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SynuSight Biotech is committed to pioneering transformative diagnostic and therapeutic molecules for neurodegenerative diseases through cutting-edge scientific expertise and innovative technology platforms, ultimately benefiting millions of patients worldwide.

SynuSight team specializes in studying the misfolding and pathological aggregation of proteins such as α-Syn, tau, and Aβ. By integrating cutting-edge technologies like Cryo-EM electron diffraction, Helical filament imaging, and In-cell NMR spectroscopy, we have built unparalleled expertise in key neurodegenerative disease targets, unlocking new possibilities for innovative therapeutic molecule development.

SynuSight has developed 18F-FD4, a novel small-molecule tracer with a unique core structure, through its structure-driven drug discovery platform combining systematic studies of ligand-α-Syn interactions with advanced AI and CADD approaches. Early investigator-initiated trials (IIT) have demonstrated its excellent blood-brain barrier penetration and superior imaging performance in both Parkinson's disease (PD) and multiple system atrophy (MSA) patients.

Our Team

Management Team

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Cong LIU

Founder & Chief Scientific Officer

Fully responsible for the company's scientific development strategy.

Bachelor's degree from Jilin University, Ph.D. from Peking University, Postdoctoral fellow at University of California, Los Angeles & Howard Hughes Medical Institute. Returned to China in 2013 and joined the Center for Chemical and Biological Sciences at the Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences, serving as a researcher and doctoral supervisor.

Dr. Cong Liu's research focuses on the use of chemical and biological interdisciplinary methods to study the mechanism of protein self-assembly and aggregation and its pathogenic role in neurodegenerative diseases. Research is conducted in three directions: the structural basis of pathological protein aggregation, the mechanism of interaction between chemical molecules and protein aggregates, and the development of molecular probes targeting pathological protein aggregation. In the past five years, more than 80 SCI papers have been published related to this work.

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Mengqi FAN

Board Member & Chief Executive Officer

Fully responsible for the global strategic planning, business development, and company operations of SynuSight Biotech.

Mr. Mengqi Fan graduated from Fudan University and has extensive experience in enterprise management and project operations, with many years of research and professional experience in bioinformatics and artificial intelligence. Before joining SynuSight Biotech, he served as the Vice President of the Biopharmaceutical Business Group at Shenshi Technology, responsible for the company's early product operations and external cooperation. During his tenure, he led the team to achieve BD cooperation with hundreds of domestic and foreign innovative pharmaceutical companies and research institutions, successfully building Shenshi Technology as an industry leader in AI for Science in the biopharmaceutical field.

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Jiang BIAN

Head of the Discovery

Scientific Advisory Board

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Junying YUAN

Chairman of the Scientific Advisory Board

Provides strategic advice and academic support for the pipeline development of SynuSight.

Bachelor's degree in Biochemistry from Fudan University, Ph.D. from Harvard Medical School, studied under Nobel laureate Professor Robert Horvitz, Foreign Academician of the Chinese Academy of Sciences, Member of the National Academy of Sciences, USA, Director of the Center for Chemical and Biological Sciences at the Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences.

Academician Junying Yuan has been engaged in the study of cell death mechanisms for many years and is one of the pioneers in the field of cell death research worldwide. She is the discoverer of the world's first cell death gene, which laid the research foundation for the field of apoptosis research worldwide, prompting numerous laboratories around the world to systematically study apoptosis from different perspectives. Professor Yuan is the discoverer of programmed necrosis in cells and has explained how cell necrosis is regulated from the levels of chemical biology and cell biology. In recognition of Professor Yuan's significant contributions to the field of cell death, she has been invited by the Nobel Prize Committee to give special lectures on multiple occasions. Her work made a significant contribution to her mentor Dr. H.R. Horvitz's receipt of the 2002 Nobel Prize. She has received various international outstanding research awards such as the Ryan Fellowship, Wilson S. Stone Memorial Award, The SCBA Outstanding Young Investigator Award, and is recognized as an authority in the field of cell death research by the international academic community.

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Dan LI

Scientific Advisory Board Member

Vice President of the School of Life Sciences and Technology, Shanghai Jiao Tong University, Executive Dean of Bio-X Research Institute, Young Talent of the Ten Thousand Talents Program. Professor Dan Li's research focuses on the role of pathological protein phase separation/phase transition in neurodegenerative diseases and the study of tracing and regulating pathological protein phase transition aggregation through chemical means.

Developing and applying biophysical, biochemical, and cell biological techniques to elucidate the molecular mechanisms by which protein phase regulation disorders lead to abnormal aggregation and the formation of pathological aggregates, and their relationship with neurodegenerative diseases, revealing the pathogenic mechanisms of abnormal aggregation of key pathogenic proteins in various neurodegenerative diseases, and achieving in situ tracing of pathological protein aggregates through rational design of chemical molecules. The molecular tracers developed are currently in preclinical development. In the past five years, Professor Dan Li has published more than 60 SCI papers, cited more than 3,500 times (Google Scholar). As (co-)corresponding author, he has published more than 30 SCI papers in high-level journals such as Cell, Cell Research, Cell Reports, PNAS, Nature Chemical Biology, Nature Structural & Molecular Biology, Nature Communications, eLife. He has successively presided over major integrated projects and general projects of the National Natural Science Foundation of China.

Our Research

2024.11.11
Journal of Biological Chemistry

Different charged biopolymers induce α-synuclein to form fibrils with distinct structures

This research offers valuable insights into how various charged biopolymers affect the aggregation process and the resultant structures of α-Syn fibrils, thereby enhancing our understanding of the structural variations in α-Syn fibrils across different pathological conditions.

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2024.10.17
Nature Structural & Molecular Biology

Time-course remodeling and pathology intervention of α-synuclein amyloid fibril by heparin and heparin-like oligosaccharides

This study reveals that heparin polysaccharides bind to α-synuclein fibrils, remodel their structure, and play a role in disease progression. It pioneers using bioactive oligosaccharides to regulate protein aggregation and toxicity, offering new strategies for drug development targeting neurodegenerative disease aggregates.

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2024.9.27
Journal of the American Chemical Society

Inhibitor development for α-synuclein fibril's disordered region to alleviate Parkinson's disease pathology

This study designs the first small molecules targeting the disordered region of α-synuclein fibrils, blocking their interaction with cell receptors to inhibit propagation and neuroinflammation, and providing new strategies for Parkinson's disease treatment.

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2024.8.22
PNAS

Binding adaptability of chemical ligands to polymorphic α-synuclein amyloid fibrils

This study investigated the interactions of small molecules belonging to four distinct scaffolds, with different α-Syn fibril polymorphs. Using cryo-electron microscopy, we determined the structures of these molecules when bound to the fibrils formed by E46K mutant α-Syn and compared them to those bound with wild-type α-syn fibrils.

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2024.5.25
National Science Review

Lysophosphatidylcholine binds α-synuclein and prevents its pathological aggregation

This work underscores the critical role of LPLs in preserving the natural conformation of α-syn to inhibit improper aggregation, and establishes a potential connection between lipid metabolic dysfunction and α-Syn aggregation in PD.

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2023.7.7
Cell

Development of an α-synuclein positron emission tomography tracer for imaging synucleinopathies

This study identifies a brain-permeable, rapid-washout PET tracer [18F]-F0502B and resolves its 2.8 Å atomic structure in complex with α-Syn fibrils. PET imaging demonstrates its selective detection of α-Syn aggregates in mouse and non-human primate PD models, offering a novel tool for early Parkinson's disease diagnosis.

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2023.7.3
Nature Chemical Biology

Structural mechanism for specific binding of chemical compounds to amyloid fibrils

This study employs cryo-electron microscopy (cryo-EM) to systematically elucidate the structural landscape of amyloid fibril interactions with a diverse panel of compounds, including classic dyes, (pre)clinically imaging tracers and newly identified binders from high-throughput screening. This study holds significant implications for the development of new diagnostic and therapeutic approaches for neurodegenerative diseases.

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2024.2.16
Journal of the American Chemical Society

Conformational dynamics of an α-synuclein fibril upon receptor binding revealed by insensitive nuclei enhanced by polarization transfer-based solid-state nuclear magnetic resonance and cryo-electron microscopy

This study deciphers how LAG3 binds to α-Syn fibrils' terminal domains, triggering core region remodeling at atomic resolution.

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2022.9.20
Cell Reports

Interaction of RAGE with α-synuclein fibrils mediates inflammatory response of microglia

This study reveals that pathological α-Syn fibrils induce microglial inflammatory responses by directly binding to the RAGE receptor on the cell surface. It also elucidates the molecular mechanism of RAGE recognition of α-Syn fibrils. This work provides a potential new therapeutic target for Parkinson's disease (PD) by inhibiting neuroinflammation.

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2021.5.25
PNAS

Mechanistic basis for receptor-mediated pathological α-synuclein fibril cell-to-cell transmission in Parkinson's disease

This work reveals the important role of post-translational modification in cell-to-cell transmission of α-Syn pathological fibrils in inducing pathological toxicity, and provides new ideas for the development of PD drugs.

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