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UV-modulated substrate rigidity for multiscale study of mechanoresponsive cellular behaviors.

ABSTRACT: Mechanical properties of the extracellular matrix (ECM) have profound effects on cellular functions. Here, we applied novel photosensitive polydimethylsiloxane (photoPDMS) chemistry to create photosensitive, biocompatible photoPDMS as a rigidity-tunable material for study of mechanoresponsive cellular behaviors. By modulating the PDMS cross-linker to monomer ratio, UV light exposure time, and postexposure baking time, we achieved a broad range of bulk Young's modulus for photoPDMS from 0.027 to 2.48 MPa. Biocompatibility of photoPDMS was assayed, and no significant cytotoxic effect was detected as compared to conventional PDMS. We demonstrated that the bulk Young's modulus of photoPDMS could impact cell morphology, adhesion formation, cytoskeletal structure, and cell proliferation. We further fabricated photoPDMS micropost arrays for multiscale study of mechanoresponsive cellular behaviors. Our results suggested that adherent cells could sense and respond to changes of substrate rigidity at a subfocal adhesion resolution. Together, we demonstrated the potential of photoPDMS as a photosensitive and rigidity-tunable material for mechanobiology studies.

SUBMITTER: Sun Y

PROVIDER: S-EPMC4123631 | biostudies-literature | 2012 Jul

REPOSITORIES: biostudies-literature

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UV-modulated substrate rigidity for multiscale study of mechanoresponsive cellular behaviors.

Sun Yubing Y Jiang Liang-Ting LT Okada Ryoji R Fu Jianping J

Langmuir : the ACS journal of surfaces and colloids 20120712 29

Mechanical properties of the extracellular matrix (ECM) have profound effects on cellular functions. Here, we applied novel photosensitive polydimethylsiloxane (photoPDMS) chemistry to create photosensitive, biocompatible photoPDMS as a rigidity-tunable material for study of mechanoresponsive cellular behaviors. By modulating the PDMS cross-linker to monomer ratio, UV light exposure time, and postexposure baking time, we achieved a broad range of bulk Young's modulus for photoPDMS from 0.027 to ...[more]

PMID: 22742430

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Project description:The emerging complexity of large macromolecules has led to challenges in their full scale theoretical description and computer simulation. Multiscale multiphysics and multidomain models have been introduced to reduce the number of degrees of freedom while maintaining modeling accuracy and achieving computational efficiency. A total energy functional is constructed to put energies for polar and nonpolar solvation, chemical potential, fluid flow, molecular mechanics, and elastic dynamics on an equal footing. The variational principle is utilized to derive coupled governing equations for the above mentioned multiphysical descriptions. Among these governing equations is the Poisson-Boltzmann equation which describes continuum electrostatics with atomic charges. The present work introduces the theory of continuum elasticity with atomic rigidity (CEWAR). The essence of CEWAR is to formulate the shear modulus as a continuous function of atomic rigidity. As a result, the dynamics complexity of a macromolecular system is separated from its static complexity so that the more time-consuming dynamics is handled with continuum elasticity theory, while the less time-consuming static analysis is pursued with atomic approaches. We propose a simple method, flexibility-rigidity index (FRI), to analyze macromolecular flexibility and rigidity in atomic detail. The construction of FRI relies on the fundamental assumption that protein functions, such as flexibility, rigidity, and energy, are entirely determined by the structure of the protein and its environment, although the structure is in turn determined by all the interactions. As such, the FRI measures the topological connectivity of protein atoms or residues and characterizes the geometric compactness of the protein structure. As a consequence, the FRI does not resort to the interaction Hamiltonian and bypasses matrix diagonalization, which underpins most other flexibility analysis methods. FRI's computational complexity is of O(N(2)) at most, where N is the number of atoms or residues, in contrast to O(N(3)) for Hamiltonian based methods. We demonstrate that the proposed FRI gives rise to accurate prediction of protein B-Factor for a set of 263 proteins. We show that a parameter free FRI is able to achieve about 95% accuracy of the parameter optimized FRI. An interpolation algorithm is developed to construct continuous atomic flexibility functions for visualization and use with CEWAR.

Dataset Information

UV-modulated substrate rigidity for multiscale study of mechanoresponsive cellular behaviors.

Publications

UV-modulated substrate rigidity for multiscale study of mechanoresponsive cellular behaviors.

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