ArticleBiomolecules2019
Systematic FTIR Spectroscopy Study of the Secondary Structure Changes in Human Serum Albumin under Various Denaturation Conditions.
Article in Biomolecules, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 65 papers.
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Who cites it
65 citing papers in PubMed, 212 citations in OpenAlex.
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- Lipid Composition Modulates Secondary Structure at the Biocondensate-Membrane Interface.bioRxiv : the preprint server for biology · 2026Article
- Ultrasound-Assisted Curdlan Curing Reduces Water Loss of Rabbit Meat: Water Retention Performance, Myofibrillar Protein Structure, and Processing Adaptability.Foods (Basel, Switzerland) · 2026Article
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- Synthesis and Characterization of Rubisco-Magnesium Complexes for Potential Gas Adsorption Applications.ACS omega · 2026Article
- Impacts of Single and Sequential Enzymatic Extraction on the Functional Properties of Khao Dawk Mali 105 Rice Bran Proteins at Two Maturity Stages.Foods (Basel, Switzerland) · 2026Article
- An organolutetium nanosensitizer synergizes with PARP inhibition to unleash STING-mediated immunity for low-dose radioimmunotherapy.Theranostics · 2026Article
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- Preparation of Self-Assembled Human Serum Albumin Nanoparticles Decorated with Trastuzumab as a Paclitaxel Delivery System.Micromachines · 2025Article
- Electrostatic Targeting of Cancer Cell Membrane Models by NA-CATH:ATRA-1-ATRA-1: A Biophysical Perspective.Membranes · 2025Article
- Spectroscopic analyses for possible transport of polyaromatic hydrocarbons onto fish in Mediterranean Sea.Scientific reports · 2025Article
- Structural Properties and Stability of Proteins in Dihydrolevoglucosenone/Water Mixtures.The journal of physical chemistry. B · 2025Article
5 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Human serum albumin (HSA) is the most abundant protein in blood plasma. HSA is involved in the transport of hormones, fatty acids, and some other compounds, maintenance of blood pH, osmotic pressure, and many other functions. Although this protein is well studied, data about its conformational changes upon different denaturation factors are fragmentary and sometimes contradictory. This is especially true for FTIR spectroscopy data interpretation. Here, the effect of various denaturing agents on the structural state of HSA by using FTIR spectroscopy in the aqueous solutions was systematically studied. Our data suggest that the second derivative deconvolution method provides the most consistent interpretation of the obtained IR spectra. The secondary structure changes of HSA were studied depending on the concentration of the denaturing agent during acid, alkaline, and thermal denaturation. In general, the denaturation of HSA in different conditions is accompanied by a decrease in α-helical conformation and an increase in random coil conformation and the intermolecular β-strands. Meantime, some variation in the conformational changes depending on the type of the denaturation agent were also observed. The increase of β-structural conformation suggests that HSA may form amyloid-like aggregates upon the denaturation.
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