Cytoskeletal Polymer Networks: Viscoelastic Properties are Determined by the Microscopic Interaction Potential of Cross-links

O. Lieleg, K.M. Schmoller, Mireille Maria Anna Elisabeth Claessens, A.R. Bausch

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Abstract

Although the structure of cross-linking molecules mainly determines the structural organization of actin filaments and with that the static elastic properties of the cytoskeleton, it is largely unknown how the biochemical characteristics of transiently cross-linking proteins (actin-binding proteins (ABPs)) affect the viscoelasticity of actin networks. In this study, we show that the macroscopic network response of reconstituted actin networks can be traced back to the microscopic interaction potential of an individual actin/ABP bond. The viscoelastic response of cross-linked actin networks is set by the cross-linker off-rate, the binding energy, and the characteristic bond length of individual actin/ABP interactions.
Original languageEnglish
Pages (from-to)4725-4732
Number of pages8
JournalBiophysical journal
Volume96
Issue number3
DOIs
Publication statusPublished - 2009

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Actins
Polymers
Microfilament Proteins
Cytoskeleton
Actin Cytoskeleton
Proteins

Cite this

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title = "Cytoskeletal Polymer Networks: Viscoelastic Properties are Determined by the Microscopic Interaction Potential of Cross-links",
abstract = "Although the structure of cross-linking molecules mainly determines the structural organization of actin filaments and with that the static elastic properties of the cytoskeleton, it is largely unknown how the biochemical characteristics of transiently cross-linking proteins (actin-binding proteins (ABPs)) affect the viscoelasticity of actin networks. In this study, we show that the macroscopic network response of reconstituted actin networks can be traced back to the microscopic interaction potential of an individual actin/ABP bond. The viscoelastic response of cross-linked actin networks is set by the cross-linker off-rate, the binding energy, and the characteristic bond length of individual actin/ABP interactions.",
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Cytoskeletal Polymer Networks: Viscoelastic Properties are Determined by the Microscopic Interaction Potential of Cross-links. / Lieleg, O.; Schmoller, K.M.; Claessens, Mireille Maria Anna Elisabeth; Bausch, A.R.

In: Biophysical journal, Vol. 96, No. 3, 2009, p. 4725-4732.

Research output: Contribution to journalArticleAcademicpeer-review

TY - JOUR

T1 - Cytoskeletal Polymer Networks: Viscoelastic Properties are Determined by the Microscopic Interaction Potential of Cross-links

AU - Lieleg, O.

AU - Schmoller, K.M.

AU - Claessens, Mireille Maria Anna Elisabeth

AU - Bausch, A.R.

PY - 2009

Y1 - 2009

N2 - Although the structure of cross-linking molecules mainly determines the structural organization of actin filaments and with that the static elastic properties of the cytoskeleton, it is largely unknown how the biochemical characteristics of transiently cross-linking proteins (actin-binding proteins (ABPs)) affect the viscoelasticity of actin networks. In this study, we show that the macroscopic network response of reconstituted actin networks can be traced back to the microscopic interaction potential of an individual actin/ABP bond. The viscoelastic response of cross-linked actin networks is set by the cross-linker off-rate, the binding energy, and the characteristic bond length of individual actin/ABP interactions.

AB - Although the structure of cross-linking molecules mainly determines the structural organization of actin filaments and with that the static elastic properties of the cytoskeleton, it is largely unknown how the biochemical characteristics of transiently cross-linking proteins (actin-binding proteins (ABPs)) affect the viscoelasticity of actin networks. In this study, we show that the macroscopic network response of reconstituted actin networks can be traced back to the microscopic interaction potential of an individual actin/ABP bond. The viscoelastic response of cross-linked actin networks is set by the cross-linker off-rate, the binding energy, and the characteristic bond length of individual actin/ABP interactions.

U2 - 10.1016/j.bpj.2009.03.038

DO - 10.1016/j.bpj.2009.03.038

M3 - Article

VL - 96

SP - 4725

EP - 4732

JO - Biophysical journal

JF - Biophysical journal

SN - 0006-3495

IS - 3

ER -