Key residues regulating von Willebrand factor A1/A2 interactions: insights from molecular dynamics simulations and experimental validation
By integrating computational prediction with experimental validation, we identified residues D1323, R1334, and Q1367 on A1, along with V1546, R1575, and E1598 on A2, as key residues that maintain the A1/A2 interaction. These findings enhance our understanding of the VWF-A1/A2 interaction mechanism and provide novel molecular targets and a theoretical basis for developing targeted therapies for associated disorders.
Authors
- Yu‐ming M. Huang (ORCID: https://orcid.org/0000-0003-3257-6170)
- Àiyīng Liú
- Jiangguo Lin (ORCID: https://orcid.org/0000-0002-1373-3268)
- Zhiwei Wu (ORCID: https://orcid.org/0000-0002-0672-948X)
- J. Fang (ORCID: https://orcid.org/0009-0005-3609-8067)
- Junxian Yang (ORCID: https://orcid.org/0009-0005-5965-7167)
Institutions
- Guangdong Academy of Medical Sciences (CN)
- Southern Medical University (CN)
- South China University of Technology (CN)
Publication Details
- Journal
- Research and Practice in Thrombosis and Haemostasis
- Published
- 2025-11-01
- DOI
- https://doi.org/10.1016/j.rpth.2025.103267
- Primary Topic
- Platelet Disorders and Treatments
- Type
- article
- Field-Weighted Citation Impact
- 0.00
Funders
- National Natural Science Foundation of China
- Natural Science Foundation of Guangdong Province
- Guangzhou Municipal Science and Technology Project