Nanoscale Molecular Quantification of Stem Cell–Hydrogel Interactions
Author(s) -
Stephanie A. Maynard,
Amy Gelmi,
Stacey C. Skaalure,
Isaac J. Pence,
C. Lee-Reeves,
Julia Sero,
Thomas E. Whittaker,
Molly M. Stevens
Publication year - 2020
Publication title -
acs nano
Language(s) - Uncategorized
Resource type - Journals
SCImago Journal Rank - 5.554
H-Index - 382
eISSN - 1936-086X
pISSN - 1936-0851
DOI - 10.1021/acsnano.0c07428
Subject(s) - self healing hydrogels , force spectroscopy , mesenchymal stem cell , cell adhesion , materials science , biomaterial , nanotechnology , regenerative medicine , integrin , tissue engineering , biophysics , nanoscopic scale , cell , adhesion , stem cell , chemistry , microbiology and biotechnology , atomic force microscopy , biomedical engineering , biochemistry , biology , medicine , polymer chemistry , composite material
A common approach to tailoring synthetic hydrogels for regenerative medicine applications involves incorporating RGD cell adhesion peptides, yet assessing the cellular response to engineered microenvironments at the nanoscale remains challenging. To date, no study has demonstrated how RGD concentration in hydrogels affects the presentation of individual cell surface receptors. Here we studied the interaction between human mesenchymal stem cells (hMSCs) and RGD-functionalized poly(ethylene glycol) hydrogels, by correlating macro- and nanoscale single-cell interfacial quantification techniques. We quantified RGD unbinding forces on a synthetic hydrogel using single cell atomic force spectroscopy, revealing that short-term binding of hMSCs was sensitive to RGD concentration. We also performed direct stochastic optical reconstruction microscopy (dSTORM) to quantify the molecular interactions between integrin α5β1 and a biomaterial, unexpectedly revealing that increased integrin clustering at the hydrogel-cell interface correlated with fewer available RGD binding sites. Our complementary, quantitative approach uncovered mechanistic insights into specific stem cell-hydrogel interactions, where dSTORM provides nanoscale sensitivity to RGD-dependent differences in cell surface localization of integrin α5β1. Our findings reveal that it is possible to precisely determine how peptide-functionalized hydrogels interact with cells at the molecular scale, thus providing a basis to fine-tune the spatial presentation of bioactive ligands.
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