Measurement of Elastic Modulus of Collagen Type I Single Fiber.

Collagen fibers are the main components of the extra cellular matrix and the primary contributors to the mechanical properties of tissues. Here we report a novel approach to measure the longitudinal component of the elastic moduli of biological fibers under conditions close to those found in vivo an...

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Main Authors: Pavel Dutov, Olga Antipova, Sameer Varma, Joseph P R O Orgel, Jay D Schieber
Format: Article
Language:English
Published: Public Library of Science (PLoS) 2016-01-01
Series:PLoS ONE
Online Access:http://europepmc.org/articles/PMC4723153?pdf=render
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spelling doaj-83e377b0b9394534b0a4fc21f20c53e72020-11-24T21:52:03ZengPublic Library of Science (PLoS)PLoS ONE1932-62032016-01-01111e014571110.1371/journal.pone.0145711Measurement of Elastic Modulus of Collagen Type I Single Fiber.Pavel DutovOlga AntipovaSameer VarmaJoseph P R O OrgelJay D SchieberCollagen fibers are the main components of the extra cellular matrix and the primary contributors to the mechanical properties of tissues. Here we report a novel approach to measure the longitudinal component of the elastic moduli of biological fibers under conditions close to those found in vivo and apply it to type I collagen from rat tail tendon. This approach combines optical tweezers, atomic force microscopy, and exploits Euler-Bernoulli elasticity theory for data analysis. This approach also avoids drying for measurements or visualization, since samples are freshly extracted. Importantly, strains are kept below 0.5%, which appear consistent with the linear elastic regime. We find, surprisingly, that the longitudinal elastic modulus of type I collagen cannot be represented by a single quantity but rather is a distribution that is broader than the uncertainty of our experimental technique. The longitudinal component of the single-fiber elastic modulus is between 100 MPa and 360 MPa for samples extracted from different rats and/or different parts of a single tail. Variations are also observed in the fibril-bundle/fibril diameter with an average of 325±40 nm. Since bending forces depend on the diameter to the fourth power, this variation in diameter is important for estimating the range of elastic moduli. The remaining variations in the modulus may be due to differences in composition of the fibril-bundles, or the extent of the proteoglycans constituting fibril-bundles, or that some single fibrils may be of fibril-bundle size.http://europepmc.org/articles/PMC4723153?pdf=render
collection DOAJ
language English
format Article
sources DOAJ
author Pavel Dutov
Olga Antipova
Sameer Varma
Joseph P R O Orgel
Jay D Schieber
spellingShingle Pavel Dutov
Olga Antipova
Sameer Varma
Joseph P R O Orgel
Jay D Schieber
Measurement of Elastic Modulus of Collagen Type I Single Fiber.
PLoS ONE
author_facet Pavel Dutov
Olga Antipova
Sameer Varma
Joseph P R O Orgel
Jay D Schieber
author_sort Pavel Dutov
title Measurement of Elastic Modulus of Collagen Type I Single Fiber.
title_short Measurement of Elastic Modulus of Collagen Type I Single Fiber.
title_full Measurement of Elastic Modulus of Collagen Type I Single Fiber.
title_fullStr Measurement of Elastic Modulus of Collagen Type I Single Fiber.
title_full_unstemmed Measurement of Elastic Modulus of Collagen Type I Single Fiber.
title_sort measurement of elastic modulus of collagen type i single fiber.
publisher Public Library of Science (PLoS)
series PLoS ONE
issn 1932-6203
publishDate 2016-01-01
description Collagen fibers are the main components of the extra cellular matrix and the primary contributors to the mechanical properties of tissues. Here we report a novel approach to measure the longitudinal component of the elastic moduli of biological fibers under conditions close to those found in vivo and apply it to type I collagen from rat tail tendon. This approach combines optical tweezers, atomic force microscopy, and exploits Euler-Bernoulli elasticity theory for data analysis. This approach also avoids drying for measurements or visualization, since samples are freshly extracted. Importantly, strains are kept below 0.5%, which appear consistent with the linear elastic regime. We find, surprisingly, that the longitudinal elastic modulus of type I collagen cannot be represented by a single quantity but rather is a distribution that is broader than the uncertainty of our experimental technique. The longitudinal component of the single-fiber elastic modulus is between 100 MPa and 360 MPa for samples extracted from different rats and/or different parts of a single tail. Variations are also observed in the fibril-bundle/fibril diameter with an average of 325±40 nm. Since bending forces depend on the diameter to the fourth power, this variation in diameter is important for estimating the range of elastic moduli. The remaining variations in the modulus may be due to differences in composition of the fibril-bundles, or the extent of the proteoglycans constituting fibril-bundles, or that some single fibrils may be of fibril-bundle size.
url http://europepmc.org/articles/PMC4723153?pdf=render
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