Self-assembly of collagen molecules into fibrils in solution

Andrew McCluskey; Julien Sindt; Andrew Young; Nico A.J.M. Sommerdijk; Paul Murray; Philip J. Camp; Fabio Nudelman

Self-assembly of collagen molecules into fibrils in solution

Andrew McCluskey, Julien Sindt, Andrew Young, Nico A.J.M. Sommerdijk, Paul Murray, Philip J. Camp, Fabio Nudelman

Electronic And Electrical Engineering

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Abstract

Type I collagen is a major constituent of many biological tissues, including skin, bone, tendon and cartilages. Its main functions are to shape extracellular matrices, promote cell attachment and provide tissues with strength, flexibility and elasticity. At the core these functions is its remarkable ability of collagen to form highly organized fibrils through the self-assembly of the molecules. The fibrilogenesis involves the lateral association of collagen triple helices into staggered parallel arrays that give rise to the characteristic D-band periodicity of 67 nm. Currently, the mechanisms of collagen self-assembly are poorly understood. Here, we combine the nanometer-scale resolution of cryo-transmission electron microscopy (cryoTEM) with molecular dynamics to investigate the self-assembly of collagen molecules into fibrils in solution.

Original language	English
Number of pages	1
Publication status	Published - 14 Aug 2016
Event	Gordon Conference on Biomineralisation - Barcelona, Spain Duration: 14 Aug 2016 → 19 Oct 2016

Conference

Conference	Gordon Conference on Biomineralisation
Country/Territory	Spain
City	Barcelona
Period	14/08/16 → 19/10/16

Keywords

collagen
fibrils
fibrologenesis

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title = "Self-assembly of collagen molecules into fibrils in solution",

abstract = "Type I collagen is a major constituent of many biological tissues, including skin, bone, tendon and cartilages. Its main functions are to shape extracellular matrices, promote cell attachment and provide tissues with strength, flexibility and elasticity. At the core these functions is its remarkable ability of collagen to form highly organized fibrils through the self-assembly of the molecules. The fibrilogenesis involves the lateral association of collagen triple helices into staggered parallel arrays that give rise to the characteristic D-band periodicity of 67 nm. Currently, the mechanisms of collagen self-assembly are poorly understood. Here, we combine the nanometer-scale resolution of cryo-transmission electron microscopy (cryoTEM) with molecular dynamics to investigate the self-assembly of collagen molecules into fibrils in solution.",

keywords = "collagen, fibrils, fibrologenesis",

author = "Andrew McCluskey and Julien Sindt and Andrew Young and Sommerdijk, {Nico A.J.M.} and Paul Murray and Camp, {Philip J.} and Fabio Nudelman",

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TY - CONF

T1 - Self-assembly of collagen molecules into fibrils in solution

AU - McCluskey, Andrew

AU - Sindt, Julien

AU - Young, Andrew

AU - Sommerdijk, Nico A.J.M.

AU - Murray, Paul

AU - Camp, Philip J.

AU - Nudelman, Fabio

PY - 2016/8/14

Y1 - 2016/8/14

N2 - Type I collagen is a major constituent of many biological tissues, including skin, bone, tendon and cartilages. Its main functions are to shape extracellular matrices, promote cell attachment and provide tissues with strength, flexibility and elasticity. At the core these functions is its remarkable ability of collagen to form highly organized fibrils through the self-assembly of the molecules. The fibrilogenesis involves the lateral association of collagen triple helices into staggered parallel arrays that give rise to the characteristic D-band periodicity of 67 nm. Currently, the mechanisms of collagen self-assembly are poorly understood. Here, we combine the nanometer-scale resolution of cryo-transmission electron microscopy (cryoTEM) with molecular dynamics to investigate the self-assembly of collagen molecules into fibrils in solution.

AB - Type I collagen is a major constituent of many biological tissues, including skin, bone, tendon and cartilages. Its main functions are to shape extracellular matrices, promote cell attachment and provide tissues with strength, flexibility and elasticity. At the core these functions is its remarkable ability of collagen to form highly organized fibrils through the self-assembly of the molecules. The fibrilogenesis involves the lateral association of collagen triple helices into staggered parallel arrays that give rise to the characteristic D-band periodicity of 67 nm. Currently, the mechanisms of collagen self-assembly are poorly understood. Here, we combine the nanometer-scale resolution of cryo-transmission electron microscopy (cryoTEM) with molecular dynamics to investigate the self-assembly of collagen molecules into fibrils in solution.

KW - collagen

KW - fibrils

KW - fibrologenesis

UR - https://www.grc.org

M3 - Poster

T2 - Gordon Conference on Biomineralisation

Y2 - 14 August 2016 through 19 October 2016

ER -

Self-assembly of collagen molecules into fibrils in solution

Abstract

Conference

Keywords

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