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1.
Biophys J ; 99(12): L94-6, 2010 Dec 15.
Article in English | MEDLINE | ID: mdl-21156124

ABSTRACT

Efforts to understand and engineer cell behavior in mechanically soft environments frequently employ two-dimensional cell culture substrates consisting of thin hydrogel layers with low elastic modulus supported on rigid substrates to facilitate culturing, imaging, and analysis. Here we characterize how an elastic creasing instability of the gel surface may occur for the most widely used soft cell culture substrate, polyacrylamide hydrogels, and show that stem cells respond to and change their behavior due to these surface features. The regions of stability and corresponding achievable ranges of modulus are elucidated in terms of the monomer and cross-linker concentrations, providing guidance for the synthesis of both smooth and creased soft cell substrates for basic and applied cell engineering efforts.


Subject(s)
Acrylic Resins/chemistry , Acrylic Resins/pharmacology , Neural Stem Cells/cytology , Neural Stem Cells/drug effects , Adult Stem Cells/cytology , Adult Stem Cells/drug effects , Cells, Cultured , Elastic Modulus/drug effects , Microscopy, Phase-Contrast , Neurites/drug effects , Neurites/metabolism , Surface Properties/drug effects
2.
Biophys J ; 98(4): 657-66, 2010 Feb 17.
Article in English | MEDLINE | ID: mdl-20159162

ABSTRACT

Decomposition of the intrinsic dynamics of proteins into collective motions among distant regions of the protein structure provides a physically appealing approach that couples the dynamics of the system with its functional role. The cellular functions of microtubules (an essential component of the cytoskeleton in all eukaryotic cells) depend on their dynamic instability, which is altered by various factors among which applied forces are central. To shed light on the coupling between forces and the dynamic instability of microtubules, we focus on the investigation of the response of the microtubule subunits (tubulin) to applied forces. We address this point by adapting an approach designed to survey correlations for the equilibrium dynamics of proteins to the case of correlations for proteins forced-dynamics. The resulting collective motions in tubulin have a number of functional implications, such as the identification of long-range couplings with a role in blocking the dynamic instability of microtubules. A fundamental implication of our study for the life of a cell is that, to increase the likelihood of unraveling of large cytoskeletal filaments under physiological forces, molecular motors must use a combination of pulling and torsion rather than just pulling.


Subject(s)
Movement , Tubulin/chemistry , Tubulin/metabolism , Biomechanical Phenomena , Cluster Analysis , Models, Molecular , Protein Denaturation , Protein Multimerization , Protein Structure, Quaternary , Protein Structure, Tertiary , Rotation
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