ArticleNature nanotechnology2016
Measuring protein isoelectric points by AFM-based force spectroscopy using trace amounts of sample.
Article in Nature nanotechnology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed.
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- Nanocellulose-Bovine Serum Albumin Interactions in an Aqueous Medium: Investigations Using In Situ Nanocolloidal Probe Microscopy and Reactive Molecular Dynamics Simulations.Biomacromolecules · 2024Article
- Mobile Point-of-Care Device Using Molecularly Imprinted Polymer-Based Chemosensors Targeting Interleukin-1β Biomarker.Biosensors · 2023Article
- Atomic force and infrared spectroscopic studies on the role of surface charge for the anti-biofouling properties of polydopamine films.Analytical and bioanalytical chemistry · 2023Article
- Single-Particle Characterization of SARS-CoV-2 Isoelectric Point and Comparison to Variants of Interest.Microorganisms · 2021Article
- Towards a Comprehensive and Robust Micromanipulation System with Force-Sensing and VR Capabilities.Micromachines · 2021Article
- Application of atomic force microscope in diagnosis of single cancer cells.Biomicrofluidics · 2020Review
- Integrative Transcriptome and Proteome Analysis of the Tube Foot and Adhesive Secretions of the Sea UrchinInternational journal of molecular sciences · 2020Article
- Brush Swelling and Attachment Strength of Barnacle Adhesion Protein on Zwitterionic Polymer Films as a Function of Macromolecular Structure.Langmuir : the ACS journal of surfaces and colloids · 2019Article
- Nanobiotechnology: Net charge of trace proteins.Nature nanotechnology · 2016Article
- Calcium-dependent Protein Kinases in Malaria Parasite Development and Infection.Cell transplantationArticle
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7 authors.
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No grant is acknowledged in the PubMed record.
Abstract
Protein charge at various pH and isoelectric point (pI) values is important in understanding protein function. However, often only trace amounts of unknown proteins are available and pI measurements cannot be obtained using conventional methods. Here, we show a method based on the atomic force microscope (AFM) to determine pI using minute quantities of proteins. The protein of interest is immobilized on AFM colloidal probes and the adhesion force of the protein is measured against a positively and a negatively charged substrate made by layer-by-layer deposition of polyelectrolytes. From the AFM force-distance curves, pI values with an estimated accuracy of ±0.25 were obtained for bovine serum albumin, myoglobin, fibrinogen and ribonuclease A over a range of 4.7-9.8. Using this method, we show that the pI of the 'footprint' of the temporary adhesive proteins secreted by the barnacle cyprid larvae of Amphibalanus amphitrite is in the range 9.6-9.7.
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