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| SPECIAL TOPIC — A celebration of the 90th Anniversary of the Birth of Bolin Hao |
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Force-dependent unfolding dynamics of spectrin R16: Resolving experimental contradiction and unveiling model consistency |
| Wanxing Zhang(张万星)1, Zhuwei Zhang(张珠伟)1,2, Zhenyong Xue(薛振勇)1,2, Yuhang Zhang(张宇航)1,2, Shimin Le(乐世敏)1,†, and Hu Chen(陈虎)1,2,‡ |
1 Research Institute for Biomimetics and Soft Matter, Fujian Provincial Key Laboratory for Soft Functional Materials Research, Department of Physics, Xiamen University, Xiamen 361005, China;
2 Center of Biomedical Physics, Wenzhou Institute, University of Chinese Academy of Sciences, Wenzhou 325000, China |
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Abstract Spectrin domains, characterized by a distinctive triple helix structure, are crucial in physiological processes, particularly in maintaining membrane shape and crosslinking cytoskeletons. Previous research on the 16th domain of $\alpha$-spectrin repeats (R16) has yielded conflicting results: bulk experiments showed an unfolding rate approximately two orders of magnitude faster than the zero-force result extrapolated from single-molecule force spectroscopy experiments using atomic force microscopy (AFM). To address this discrepancy, we investigated the folding and unfolding rates of R16 across a broader range of forces using magnetic tweezers (MT). Our findings reveal that AFM results at higher forces cannot be directly extrapolated to the low-force regime due to a nonlinear relationship between force and the logarithm of the unfolding rate. We demonstrated that two-dimensional model, structural-elastic model, and two-pathway model can all effectively explain the experimental data when they capture the core physics of the short unfolding distance at low forces. Our study provides a more comprehensive understanding of the unfolding dynamics of the spectrin domain, resolves previous contradictory experimental results, and highlights the common basis of different theoretical models.
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Received: 28 December 2024
Revised: 06 February 2025
Accepted manuscript online: 07 March 2025
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PACS:
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82.37.Rs
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(Single molecule manipulation of proteins and other biological molecules)
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87.14.E-
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(Proteins)
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87.15.hm
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(Folding dynamics)
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87.80.Nj
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(Single-molecule techniques)
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| Fund: Project supported by the National Natural Science Foundation of China (Grant Nos. 12174322, 12474200, 32271367, and 12204389), 111 Project (B16029), and Research Grant from Wenzhou Institute. |
Corresponding Authors:
Shimin Le, Hu Chen
E-mail: leshimin@xmu.edu.cn;chenhu@xmu.edu.cn
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Cite this article:
Wanxing Zhang(张万星), Zhuwei Zhang(张珠伟), Zhenyong Xue(薛振勇), Yuhang Zhang(张宇航), Shimin Le(乐世敏), and Hu Chen(陈虎) Force-dependent unfolding dynamics of spectrin R16: Resolving experimental contradiction and unveiling model consistency 2025 Chin. Phys. B 34 088708
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