ArticleMaterials (Basel, Switzerland)2019
Conductance Changes in Bovine Serum Albumin Caused by Drug-Binding Triggered Structural Transitions.
Article in Materials (Basel, Switzerland), 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
8 citing papers in PubMed, 28 citations in OpenAlex.
- Real-time electrical monitoring of enzymatic catalytic dynamics at the single-molecule level.Nature communications · 2026Article
- Single-Molecule Conductance of Non-Redox Proteins: Mechanisms, Measurements, and Applications.Biomolecules · 2026Review
- Autonomous Hydrogel Actuators Programmed by Endogenous Biochemical Logic for Dual-Stage Morphing and Drug Release.Advanced materials (Deerfield Beach, Fla.) · 2026Article
- Co-Surfactant-Free Bioactive Protein Nanosheets for the Stabilization of Bioemulsions Enabling Adherent Cell Expansion.Biomacromolecules · 2023Article
- Hybrid Hydrogels for Neomycin Delivery: Synergistic Effects of Natural/Synthetic Polymers and Proteins.Polymers · 2023Article
- Albumins represent highly cross-reactive animal allergens.Frontiers in immunology · 2023Review
- Improved Charge Transport across Bovine Serum Albumin-Au Nanoclusters' Hybrid Molecular Junction.ACS omega · 2022Article
- The Study of Protein-Cyclitol Interactions.International journal of molecular sciences · 2022Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Proteins, due to their binding selectivity, are promising candidates for fabricating nanoscale bio-sensors. However, the influence of structural change on protein conductance caused by specific protein-ligand interactions and disease-induced degeneration still remains unknown. Here, we excavated the relationship between circular dichroism (CD) spectroscopy and conductive atomic force microscopy (CAFM) to reveal the effect of the protein secondary structures changes on conductance. The secondary structure of bovine serum albumin (BSA) was altered by the binding of drugs, like amoxicillin (Amox), cephalexin (Cefa), and azithromycin (Azit). The CD spectroscopy shows that the α-helical and β-sheet content of BSA, which varied according to the molar ratio between the drug and BSA, changed by up to 6%. The conductance of BSA monolayers in varying drug concentrations was further characterized via CAFM. We found that BSA conductance has a monotonic relation with α-helical content. Moreover, BSA conductance seems to be in connection with the binding ability of drugs and proteins. This work elucidates that protein conductance variations caused by secondary structure transitions are triggered by drug-binding and indicate that electrical methods are of potential application in protein secondary structure analysis.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.