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

Research output: Contribution to conferencePoster

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.
LanguageEnglish
Number of pages1
Publication statusPublished - 14 Aug 2016
EventGordon Conference on Biomineralisation - Barcelona, Spain
Duration: 14 Aug 201619 Oct 2016

Conference

ConferenceGordon Conference on Biomineralisation
CountrySpain
CityBarcelona
Period14/08/1619/10/16

Fingerprint

Collagen
Self assembly
Molecules
Cryoelectron Microscopy
Tissue
Elasticity
Periodicity
Molecular Dynamics Simulation
Collagen Type I
Transmission Electron Microscopy
Tendons
Cartilage
Extracellular Matrix
Molecular dynamics
Skin
Bone
Bone and Bones
Association reactions
Transmission electron microscopy

Keywords

  • collagen
  • fibrils
  • fibrologenesis

Cite this

McCluskey, A., Sindt, J., Young, A., Sommerdijk, N. A. J. M., Murray, P., Camp, P. J., & Nudelman, F. (2016). Self-assembly of collagen molecules into fibrils in solution. Poster session presented at Gordon Conference on Biomineralisation , Barcelona, Spain.
McCluskey, Andrew ; Sindt, Julien ; Young, Andrew ; Sommerdijk, Nico A.J.M. ; Murray, Paul ; Camp, Philip J. ; Nudelman, Fabio. / Self-assembly of collagen molecules into fibrils in solution. Poster session presented at Gordon Conference on Biomineralisation , Barcelona, Spain.1 p.
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McCluskey, A, Sindt, J, Young, A, Sommerdijk, NAJM, Murray, P, Camp, PJ & Nudelman, F 2016, 'Self-assembly of collagen molecules into fibrils in solution' Gordon Conference on Biomineralisation , Barcelona, Spain, 14/08/16 - 19/10/16, .

Self-assembly of collagen molecules into fibrils in solution. / McCluskey, Andrew; Sindt, Julien; Young, Andrew; Sommerdijk, Nico A.J.M.; Murray, Paul; Camp, Philip J.; Nudelman, Fabio.

2016. Poster session presented at Gordon Conference on Biomineralisation , Barcelona, Spain.

Research output: Contribution to conferencePoster

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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

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McCluskey A, Sindt J, Young A, Sommerdijk NAJM, Murray P, Camp PJ et al. Self-assembly of collagen molecules into fibrils in solution. 2016. Poster session presented at Gordon Conference on Biomineralisation , Barcelona, Spain.