Modification of the structural stability of human serum albumin in rheumatoid arthritis

• Published in: PloS one Vol. 18; no. 3; p. e0271008
• Main Authors: Lin, Hsien-Jung L., Parkinson, David H., Holman, J. Connor, Thompson, W. Chad, Anderson, Christian N. K., Hadfield, Marcus, Ames, Stephen, Zuniga Pina, Nathan R., Bowden, Jared N., Quinn, Colette, Hansen, Lee D., Price, John C.
• Format: Journal Article
• Language: English
• Published: United States Public Library of Science 17.03.2023; Public Library of Science (PLoS)
• Subjects: Accessibility; Albumin; Amino acids; Arthritis; Arthritis, Rheumatoid; Binding; Biological products; Biological samples; Biology and Life Sciences; Biomarkers; Blood proteins; C-reactive protein; Calorimetry; Comparative analysis; Denaturation; Development and progression; Differential scanning calorimetry; Disease; Health aspects; Heat; Human serum albumin; Humans; Inflammation; Mass spectrometry; Mass spectroscopy; Medical diagnosis; Medicine and Health Sciences; Melt temperature; Patients; Peptides; Physical Sciences; Protein Binding; Protein interaction; Protein-protein interactions; Proteins; Proteomics; Research and Analysis Methods; Rheumatoid arthritis; Rheumatoid factor; Serum albumin; Serum Albumin, Human - chemistry; Serum proteins; Structural stability; Temperature; Thermal stability; United States

Differential scanning calorimetry (DSC) can indicate changes in structure and/or concentration of the most abundant proteins in a biological sample via heat denaturation curves (HDCs). In blood serum for example, HDC changes result from either concentration changes or altered thermal stabilities for...