ArticleBiophysical journal2007
Substrate chemistry-dependent conformations of single laminin molecules on polymer surfaces are revealed by the phase signal of atomic force microscopy.
Article in Biophysical journal, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed.
- Neuron-fibrous scaffold interfaces in the peripheral nervous system: a perspective on the structural requirements.Neural regeneration research · 2022Review
- Graphene-Based Scaffolds for Regenerative Medicine.Nanomaterials (Basel, Switzerland) · 2021Review
- Cost-Effective Cosmetic-Grade Hyaluronan Hydrogels for ReNcell VM Human Neural Stem Cell Culture.Biomolecules · 2019Article
- Material-driven fibronectin assembly for high-efficiency presentation of growth factors.Science advances · 2016Article
- Engineered Human Stem Cell Microenvironments.Current stem cell reports · 2016Article
- α-5 Laminin Synthesized by Human Pluripotent Stem Cells Promotes Self-Renewal.Stem cell reports · 2015Article
- A fractal nature for polymerized laminin.PloS one · 2014Article
- Synthesis and properties of caprolactone and ethylene glycol copolymers for neural regeneration.Journal of materials science. Materials in medicine · 2012Article
- Laminin Coating Promotes Calcium Phosphate Precipitation on Titanium Discs in vitro.Journal of oral & maxillofacial research · 2012Article
- In vitro Evaluation of Calcium Phosphate Precipitation on Possibly Bioactive Titanium Surfaces in the Presence of Laminin.Journal of oral & maxillofacial research · 2011Article
- Development of bioartificial myocardium using stem cells and nanobiotechnology templates.Cardiology research and practice · 2010Article
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5 authors.
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Abstract
The conformation of single laminin molecules adsorbed on synthetic substrates is directly observed making use of the phase magnitude in tapping mode atomic force microscopy (AFM). With AFM, it is not possible to differentiate the proteins on the substrate if use is made of the height signal, since the roughness of the material becomes of the same order of magnitude as the adsorbed protein, typically 10 nm height. This work shows how AFM can be exploited to reveal protein conformation on polymer materials. Different laminin morphologies are observed on a series of different copolymers based on ethyl acrylate and hydroxyethyl acrylate as a function of the surface density of -OH groups: from globular to completely extended morphologies of the protein molecules are obtained, and the onset of laminin network formation on some substrates can be clearly identified. The results stress the importance of the underlying synthetic substrate's surface chemistry for the biofunctional conformation of adsorbed proteins.
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