FRET Visualization of High Mechanosensation of von Willebrand Factor to Hydrodynamic Force

von Willebrand factor (vWF) is a large glycoprotein in the circulation system, which senses hydrodynamic force at vascular injuries and then recruits platelets in assembling clots. How vWF mechanosenses shear flow for molecular unfolding is an important topic. Here, a Förster resonance energy transfer (FRET) biosensor was developed to monitor vWF conformation change to hydrodynamic force. The vWF-based biosensor is anchored on the cell surface, in which the A2 domain is flanked with a FRET pair. With 293T cells seeded into microfluidic channels, 2.8 dyn/cm<sup>2</sup> of shear force (i.e., 28 μN/cm<sup>2</sup>, or 264.1/s in shear rate) induced a remarkable FRET change (~60%) in 30 min. A gradient micro-shear below 2.8 dyn/cm<sup>2</sup> demonstrated FRET responses positively related to flow magnitudes, with 0.14 dyn/cm<sup>2</sup> (1.4 μN/cm<sup>2</sup>) inducing an obvious change (~16%). The FRET increases indicate closer positioning of A2's two terminals in vWF or the addition of a more parallel orientation of the FRET pair, supported with the high FRET of the A2-only-based biosensor, which probably resulted from flow-induced A2 dissociation from vWF intramolecular binding such as that in A1/A3 domains. Interestingly, gradient flow increases from 2.8 to 28 dyn/cm<sup>2</sup> led to decreasing FRET changes, suggesting the second-level unfolding in the A2 domain. The LOCK-vWF biosensor with bridged A2 two terminals or an A2-only biosensor could not sense the shear, indicating a structure-flexible A2 and large vWF molecules that are important in the mechanosensation. In conclusion, the developed vWF-based biosensor demonstrated the high mechanosensation of vWF with two-level unfolding to shear force: the dissociation of the A2 domain from vWF intramolecular binding under a micro-shear, and then the unfolding of A2 in vWF under a higher shear; the FRET response to shear force at a very low scale may support the observed clot formation at microvascular wounds. This study provides new insights into the vWF's mechanosensitive feature for its physiological functions and implicated disorders.

Authors

Institutions

Publication Details

Journal
Biosensors
Published
2025-04-14
DOI
https://doi.org/10.3390/bios15040248
Primary Topic
Platelet Disorders and Treatments
Type
article
Field-Weighted Citation Impact
0.00

Funders

Controls
|||
ALL TIME
JAN
FEB
MAR
APR
MAY
JUN
JUL
AUG
SEP
OCT
article

FRET Visualization of High Mechanosensation of von Willebrand Factor to Hydrodynamic Force

Jia Guo, Mingxing Ouyang, Yingxiao Wang, Lei Lei et al.
Biosensors
Platelet Disorders and Treatments
article

FRET Visualization of High Mechanosensation of von Willebrand Factor to Hydrodynamic Force

Jia Guo, Mingxing Ouyang, Yingxiao Wang, Lei Lei, Linhong Deng, Yao Gao, Binqian Zhou
article en

Abstract

von Willebrand factor (vWF) is a large glycoprotein in the circulation system, which senses hydrodynamic force at vascular injuries and then recruits platelets in assembling clots. How vWF mechanosenses shear flow for molecular unfolding is an important topic. Here, a Förster resonance energy transfer (FRET) biosensor was developed to monitor vWF conformation change to hydrodynamic force. The vWF-based biosensor is anchored on the cell surface, in which the A2 domain is flanked with a FRET pair. With 293T cells seeded into microfluidic channels, 2.8 dyn/cm<sup>2</sup> of shear force (i.e., 28 μN/cm<sup>2</sup>, or 264.1/s in shear rate) induced a remarkable FRET change (~60%) in 30 min. A gradient micro-shear below 2.8 dyn/cm<sup>2</sup> demonstrated FRET responses positively related to flow magnitudes, with 0.14 dyn/cm<sup>2</sup> (1.4 μN/cm<sup>2</sup>) inducing an obvious change (~16%). The FRET increases indicate closer positioning of A2's two terminals in vWF or the addition of a more parallel orientation of the FRET pair, supported with the high FRET of the A2-only-based biosensor, which probably resulted from flow-induced A2 dissociation from vWF intramolecular binding such as that in A1/A3 domains. Interestingly, gradient flow increases from 2.8 to 28 dyn/cm<sup>2</sup> led to decreasing FRET changes, suggesting the second-level unfolding in the A2 domain. The LOCK-vWF biosensor with bridged A2 two terminals or an A2-only biosensor could not sense the shear, indicating a structure-flexible A2 and large vWF molecules that are important in the mechanosensation. In conclusion, the developed vWF-based biosensor demonstrated the high mechanosensation of vWF with two-level unfolding to shear force: the dissociation of the A2 domain from vWF intramolecular binding under a micro-shear, and then the unfolding of A2 in vWF under a higher shear; the FRET response to shear force at a very low scale may support the observed clot formation at microvascular wounds. This study provides new insights into the vWF's mechanosensitive feature for its physiological functions and implicated disorders.

BiosensorsVol. 15(4)
University of Southern California (US), La Jolla Bioengineering Institute (US), Changzhou University (CN)
Georgia Institute of Technology, National Natural Science Foundation of China, Changzhou University
Affordable and clean energy
Openalex Percentile: Top 90%
Platelet Disorders and Treatments
AI Navigator

Ask Laika to Summarize, Analyze, and Connect papers live on the map.

Summarize Papers & Methodologies

Extract key findings, datasets, and comparative methods across publications.

Benchmark Rankings & Visual Analytics

Rank top research institutions, authors, funders, topics, and journals by Field-Weighted Citation Impact (FWCI) and paper volume with instant charts.

Connect Distant Disciplines

Bridge topological clusters on the map to find hidden collaborative intersections.