Publication Type:

Journal Article

Source:

Advanced Healthcare Materials, Volume 2, Number 1, p.114-118 (2013)

URL:

http://www.scopus.com/inward/record.url?eid=2-s2.0-84878733337&partnerID=40&md5=49947bd300a0811ef49372be9733e3bf

Keywords:

amino acid sequence, Animals, arginylglycylaspartic acid, article, Biocompatible Materials, Biomimetic Materials, cell adhesion, cell interaction, Cross-Linking Reagents, Elastic Modulus, Elasticity, elastin, electrochemistry, Electrospinning, extracellular matrix, Humans, Materials Testing, Molecular Sequence Data, nanofabrication, nanofiber, nonhuman, Oligopeptides, priority journal, protein analysis, protein conformation, protein cross linking, protein degradation, protein depletion, Protein Engineering, protein expression, protein stability, Rotation, thermodynamics

Abstract:

A nanoscale mimic of the extracellular matrix is electrospun from a highly tunable family of elastin-like proteins. A sequence-specific, two-step crosslinking procedure is developed to preserve the nanofiber morphology, elastin-like mechanics, and specific bioactivity. Rodent marrow stromal cells show sequence-specific adhesion on the matrices, which are imaged using label-free coherent anti-Stokes Raman scattering (CARS) microscopy. © 2013 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.

Notes:

cited By 10

Cite this Research Publication

P. La Benitez, Sweet, J. Ab, Fink, Hc, Chennazhi, K. Pd, Nair, S. Vd, Enejder, Ac, and Heilshorn, S. Ce, “Sequence-Specific Crosslinking of Electrospun, Elastin-Like Protein Preserves Bioactivity and Native-Like Mechanics”, Advanced Healthcare Materials, vol. 2, pp. 114-118, 2013.

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