The hydrodynamic characteristics of heparin fractions in a 0.2 M NaCl solution have been determined. Experimental values varied over the following ranges: the sedimentation coefficient (at 20.0 degrees C), 1.3
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Heparin-binding of the human chitinase-like protein YKL-40 is allosterically modified by chitin oligosaccharides.
Biochem Biophys Rep
March 2025
Genis hf, Reykjavik, Iceland.
The chitinase-like protein YKL-40 (CHI3L1) has been implicated in the pathophysiology of inflammation and cancer. Recent studies highlight the growing interest in targeting and blocking the activity of YKL-40 to treat cancer. Some of those targeting-strategies have been developed to directly block the heparin-affinity of YKL-40 with promising results.
View Article and Find Full Text PDFUnderstanding Folding of bFGF and Potential Cellular Protective Mechanisms of Neural Cells.
Biochemistry
January 2025
Department of Chemical and Biomolecular Engineering, University of Maryland, College Park, Maryland 20742, United States.
Article Synopsis
- Traumatic brain injury (TBI) affects many individuals, especially veterans and athletes, and has serious, long-term consequences for brain health.
- Current research explores the role of fibroblast growth factor (FGF) proteins in protecting cells, highlighting knowledge gaps regarding how heparin and similar molecules activate bFGF and how mutations affect its stability.
- Using temperature replica exchange, the study identified a new binding site on bFGF and revealed that various sugars affect bFGF interactions similarly to heparin, underscoring the need for a deeper understanding of TBI mechanisms for better treatment development.
RNA G-quadruplexes and calcium ions synergistically induce Tau phase transition in vitro.
J Biol Chem
December 2024
Institute of Molecular Embryology and Genetics (IMEG), Department of Genomic Neurology, Kumamoto University, Kumamoto, Japan; Graduate School of Pharmaceutical Sciences, Kumamoto University, Kumamoto, Japan. Electronic address:
Tau aggregation is a defining feature of neurodegenerative tauopathies, including Alzheimer's disease, corticobasal degeneration, and frontotemporal dementia. This aggregation involves the liquid-liquid phase separation (LLPS) of Tau, followed by its sol-gel phase transition, representing a crucial step in aggregate formation both in vitro and in vivo. However, the precise cofactors influencing Tau phase transition and aggregation under physiological conditions (e.
View Article and Find Full Text PDFTime-course remodeling and pathology intervention of α-synuclein amyloid fibril by heparin and heparin-like oligosaccharides.
Nat Struct Mol Biol
October 2024
State Key Laboratory of Chemical Biology, Shanghai Institute of Organic Chemistry, University of Chinese Academy of Sciences, Chinese Academy of Sciences, Shanghai, China.
Article Synopsis
- Amyloid fibrils are linked to neurodegenerative diseases; polysaccharides play a key role in recognizing these fibrils and influencing their harmful effects.
- The study used cryo-electron microscopy to observe changes in the structure of α-synuclein fibrils when bound to heparin, revealing that structural alterations depend on the specific type and structure of the polysaccharides.
- Heparin-like oligosaccharides can block the spread of α-syn fibrils and inhibit their formation, highlighting potential therapeutic uses for these molecules in treating amyloid-related conditions.
High-Throughput Single-Particle Characterization of Aggregation Pathways and the Effects of Inhibitors for Large (Megadalton) Protein Oligomers.
Anal Chem
December 2024
Department of Chemistry, University of California, Berkeley, California 94720-1460, United States.
Protein aggregation is involved in many human diseases, but characterizing the sizes and shapes of intermediate oligomers (∼10-100 nm) that are important to the formation of macroscale aggregates like amyloid fibrils is a significant analytical challenge. Here, charge detection mass spectrometry (CDMS) is used to characterize individual conformational states of bovine serum albumin oligomers with up to ∼225 molecules (15 MDa). Elongated, partially folded, and globular conformational families for each oligomer can be readily distinguished based on the extent of charging.
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