Paper
12 September 2013 Probing multiscale mechanics of collagen with optical tweezers
Marjan Shayegan, Naghmeh Rezaei, Norman H. Lam, Tuba Altindal, Andrew Wieczorek, Nancy R. Forde
Author Affiliations +
Abstract
How the molecular structure of the structural, extracellular matrix protein collagen correlates with its mechanical properties at different hierarchical structural levels is not known. We demonstrate the utility of optical tweezers to probe collagen’s mechanical response throughout its assembly hierarchy, from single molecule force-extension measurements through microrheology measurements on solutions of collagen molecules, collagen fibrillar gels and gelatin. These experiments enable the determination of collagen’s flexibility, mechanics, and timescales and strengths of interaction at different levels of hierarchy, information critical to developing models of how collagen’s physiological function and stability are influenced by its chemical composition. By investigating how the viscoelastic properties of collagen are affected by the presence of telopeptides, protein domains that strongly influence fibril formation, we demonstrate that these play a role in conferring transient elasticity to collagen solutions.
© (2013) COPYRIGHT Society of Photo-Optical Instrumentation Engineers (SPIE). Downloading of the abstract is permitted for personal use only.
Marjan Shayegan, Naghmeh Rezaei, Norman H. Lam, Tuba Altindal, Andrew Wieczorek, and Nancy R. Forde "Probing multiscale mechanics of collagen with optical tweezers", Proc. SPIE 8810, Optical Trapping and Optical Micromanipulation X, 88101P (12 September 2013); https://doi.org/10.1117/12.2027258
Lens.org Logo
CITATIONS
Cited by 16 scholarly publications.
Advertisement
Advertisement
RIGHTS & PERMISSIONS
Get copyright permission  Get copyright permission on Copyright Marketplace
KEYWORDS
Collagen

Molecules

Optical tweezers

Mechanics

Molecular self-assembly

Particles

Proteins

Back to Top