Nanoparticle Tension Probes Patterned at the Nanoscale: Impact of Integrin Clustering on Force Transmission

• Type of Material: Article
• Authors: Yang Liu, Emory University; Rebecca Medda, Heidelberg University; Zheng Liu, Emory University; Kornelia Galior, Emory University; Kevin Yehl, Emory University; Joachim P. Spatz, Heidelberg University; Elisabetta Ada Cavalcanti-Adam, Heidelberg University; Khalid Salaita, Emory University
• Language: English
• Date: 2014-10-01
• Publisher: AMER CHEMICAL SOC
• Publication Version: Final Published Version
• Copyright Statement: © 2014 American Chemical Society
• License: Creative Commons Attribution-NonCommercial-NoDerivs 4.0 International
• Final Published Version (URL): http://dx.doi.org/10.1021/nl501912g
• Title of Journal or Parent Work: NANO LETTERS
• Volume: 14
• Issue: 10
• Start Page: 5539
• End Page: 5546
• Grant/Funding Information: K.S. is grateful for support from the NIH through R01-GM097399, the Alfred P. Sloan Research Fellowship, the Camille-Dreyfus Teacher-Scholar Award, and the NSF for the IDBR (1353939) and CAREER Award (1350829). E.A.C thanks the support from Max Planck Society for this work.
• Keywords: integrin; ACTIN-FILAMENTS; Nanopatterning; EXTRACELLULAR-MATRIX; ACTIVATION; Chemistry, Physical; Physical Sciences; POLYMERS; Materials Science; focal adhesion; Physics, Condensed Matter; Chemistry; Physics, Applied; molecular tension fluorescence microscopy; Physics; FOCAL ADHESIONS; Science & Technology - Other Topics; mechanotransduction; Science & Technology; MECHANICAL REGULATION; Chemistry, Multidisciplinary; receptor clustering; FIBRONECTIN; Nanoscience & Nanotechnology; Technology; MOVEMENT; REVEALS; CELL; Materials Science, Multidisciplinary
• Research Categories: Physics, General; Biology, Cell

Abstract

Herein we aimed to understand how nanoscale clustering of RGD ligands alters the mechano-regulation of their integrin receptors. We combined molecular tension fluorescence microscopy with block copolymer micelle nanolithography to fabricate substrates with arrays of precisely spaced probes that can generate a 10-fold fluorescence response to pN-forces. We found that the mechanism of sensing ligand spacing is force-mediated. This strategy is broadly applicable to investigating receptor clustering and its role in mechanotransduction pathways.