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Protein aggregation is a pathological feature in various neurodegenerative diseases and is thought to play a crucial role in the onset and progression of neurological disorders. This pathological phenomenon has attracted increasing attention from researchers, but the underlying mechanism has not been fully elucidated yet. Researchers are increasingly interested in identifying chemicals or methods that can effectively detect protein aggregation or maintain protein stability to prevent aggregation formation. To date, several methods are available for detecting protein aggregates, including fluorescence correlation spectroscopy, electron microscopy, and molecular detection methods. Unfortunately, there is still a lack of methods to observe protein aggregation in situ under a microscope. This article reviews the two main aspects of protein aggregation: the mechanisms and detection methods of protein aggregation. The aim is to provide clues for the development of new methods to study this pathological phenomenon.
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http://dx.doi.org/10.1016/j.jchemneu.2024.102420 | DOI Listing |
J Mater Chem B
September 2025
Malopolska Centre of Biotechnology, Jagiellonian University, Krakow 30-387, Poland.
Degradation during production and delivery is a significant bottleneck in developing biomolecular therapies. Protein cages, formed by engineered variants of lumazine synthase, present an effective strategy for the microbial production and isolation of labile biomolecular therapies. Genetic fusion of the target polypeptide to a cage component protomer ensures its efficient encapsulation within the cage during production in host bacterial cells, thereby protecting it from degradation.
View Article and Find Full Text PDFJ Neural Transm (Vienna)
September 2025
Department of Biomedical and Neuromotor Sciences, University of Bologna, Bologna, 40139, Italy.
Multisystem proteinopathy 1 (MSP1) is a rare autosomal dominant disorder caused by mutations in the valosin-containing protein (VCP) gene typically presenting with inclusion body myopathy (IBM), Paget's disease of bone (PDB), frontotemporal dementia (FTD), and amyotrophic lateral sclerosis (ALS). Parkinsonism is a rare feature of MSP1, occurring in 3-4% of cases, with limited post-mortem evidence suggesting neuronal synucleinopathy. We report a case of VCP-related parkinsonism providing the first in vivo demonstration of phosphorylated alpha-synuclein deposition in skin biopsy, a highly sensitive and specific in vivo biomarker of synucleinopathy.
View Article and Find Full Text PDFNature
September 2025
Institute of Materials, Ecole Polytechnique Fédérale de Lausanne, Lausanne, Switzerland.
Amino acids (AAs) have a long history of being used as stabilizers for biological media. For example, they are important components in biomedical formulations. The effect of AAs on biological systems is also starting to be appreciated.
View Article and Find Full Text PDFTrends Biochem Sci
September 2025
Department of Biochemistry and Molecular Biology, University of Nevada, Reno, NV, USA. Electronic address:
Huntington's disease (HD) is a neurodegenerative disorder caused by an expanded CAG repeat in the huntingtin (HTT) gene, resulting in an expanded polyglutamine (polyQ) tract in HTT protein. Expanded polyQ tracts cause mutant HTT (mHTT) to aggregate and accumulate as cellular inclusions. Recent studies highlight the interactions between mHTT and different cellular membranes that contribute to HD pathogenesis.
View Article and Find Full Text PDFClin Investig Arterioscler
September 2025
Cardiovascular Biochemistry, IR SANT PAU, Barcelona, Spain; CIBER of Diabetes and Metabolic Diseases (CIBERDEM), Madrid, Spain. Electronic address:
Background: Electronegative LDL (LDL(-)) is a circulant modified LDL with inflammatory properties whose proportion raises in ischemic events. The soluble form of LDL receptor related protein 1 (sLRP1) increases in blood in pathological situations, including ischemic stroke. We aimed to evaluate the effect of LDL(-) on sLRP1 release from monocytes and macrophages.
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