Visualizing molecular deformation in fibrin networks under tensile loading via FLIM-FRET

Mapping molecular deformation and forces in protein biomaterials is critical to understanding mechanochemistry. Here we use intramolecular Förster resonance energy transfer (FRET) of dual-labeled fibrin to distinguish molecular conformations of proteins during mechanical loading. The FRET approach o...

Full description

Saved in:
Bibliographic Details
Published in:Chemical communications (Cambridge, England) England), 2023-12, Vol.59 (98), p.14575-14578
Main Authors: Hedayati, Mohammadhasan, Chen, Yuan-I, Houser, Justin R, Wang, Yujen, Norouzi, Sajjad, Yeh, Hsin-Chih, Parekh, Sapun H
Format: Article
Language:English
Subjects:
Biomedical materials
Deformation
Energy transfer
Fibrin
Fluorescence Resonance Energy Transfer - methods
Green Fluorescent Proteins - chemistry
Microscopy, Fluorescence - methods
Proteins
Spatial resolution
Citations: Items that this one cites
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:Mapping molecular deformation and forces in protein biomaterials is critical to understanding mechanochemistry. Here we use intramolecular Förster resonance energy transfer (FRET) of dual-labeled fibrin to distinguish molecular conformations of proteins during mechanical loading. The FRET approach offers increased spatial resolution compared to our previous vibrational imaging. By using fluorescence lifetime microscopy (FLIM), we demonstrate that the combination of FRET and FLIM can probe the molecular changes in fibrin with high spatial (nanometer) and temporal (nanosecond) resolution. Our results map changes in fibrin monomer deformation during the macroscopic loading of the fibrin network, paving the way to directly visualizing the biomaterial mechanics and structure in cell-ECM scaffolds for the first time.
ISSN:1359-7345
1364-548X
DOI:10.1039/d3cc05281h