ArticleFrontiers in chemistry2021
Isoelectric Point of Proteins at Hydrophobic Interfaces.
Article in Frontiers in chemistry, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- Tantalum-Doped Co-Cr Alloys: Multiscale Effects on Mechanics, Surface Potential, and Biological Responses.ACS omega · 2026Article
- Simultaneous Electrochemical Detection of NGF and proNGF Under Native Conditions Using Molecularly Imprinted Polymers: Toward Point-of-Care Diagnosis of Alzheimer's Disease.Advanced healthcare materials · 2026Article
- Parametric Cyclic Voltammetric Analysis of an Electrochemical Aptasensor forMicromachines · 2025Article
- Recent innovations for improving the techno-functional properties of plant-based egg analogs and egg-mimicking products to promote their industrialization and commercialization.Comprehensive reviews in food science and food safety · 2025Review
- First identification report for amino acid composition of red algaeBiotechnologia · 2024Article
- Biocorona on Iron Oxide Nanoparticles in a Complex Biotechnological Environment: Analysis of Proteins, Lipids, and Carbohydrates.Small science · 2023Article
- Composition, Structure, and Techno-Functional Characteristics of the Flour, Protein Concentrate, and Protein Isolate from Purslane (Portulaca oleracea L.) Seeds.Plant foods for human nutrition (Dordrecht, Netherlands) · 2023Article
- Artificial Biomimetic Electrochemical Assemblies.Biosensors · 2022Review
- Effects of Relative Molecular Weight Distribution and Isoelectric Point on the Swelling Behavior of Gelatin Films.Frontiers in chemistry · 2022Article
- Effect of Surfactants on the Molecular Structure of the Buried Oil/Water Interface.Angewandte Chemie (International ed. in English) · 2021Article
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Authors and funding
3 authors.
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Abstract
Structural and colloidal stability of proteins at different surfaces and interfaces is of great importance in many fields including medical, pharmaceutical, or material science. Due to their flexibility, proteins tend to respond to their environmental conditions and can undergo structural and conformational changes. For instance, alterations in physiological factors such as temperature, ions concentration, or pH as well as the adsorption to an interface can initiate protein aggregation. Therefore, at different surfaces and interfaces the characterization of the structural and colloidal stability of proteins, which is mainly influenced by their electrostatic and hydrophobic interactions, is of fundamental importance. In this study, we utilized sum frequency generation (SFG) spectroscopy to assess the role of solution pH on the polarity and magnitude of the electric field within the hydration shell of selected model proteins adsorbed to a hydrophobic surface. We used polystyrene (PS) as a model hydrophobic surface and determined the isoelectric point (IEP) of four structurally different model proteins. Comparing the measured IEP of proteins at the PS/solution or air/solution interface with that determined in the bulk solution
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