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Neurodegenerative diseases are characterized by progressive loss of neurons manifested as motor dysfunction and/or cognitive decline. Aberrant protein aggregation with altered physicochemical properties occurs in most neurodegenerative diseases. The pathophysiological mechanisms leading to the onset and progress of neurodegenerative diseases are still not fully understood. On the one hand, limited studies investigate neurodegenerative disease from human brain tissues. On the other, a comprehensive and efficient analysis method is needed to detect the signaling pathways evolved in neurodegenerative disease. Proteomics on human brains identifies key diagnostic biomarkers and treatment/therapeutic targets of neurodegenerative disorders. In recent years, several proteomics studies conducted on brain tissues from patients with neurodegenerative diseases have shown that changes in protein abundance or post-translational modification underly the disease pathogenesis. In this review, we summarize the major advances of human brain proteomics in the research on Alzheimer’s disease, Parkinson’s disease, multiple sclerosis, amyotrophic lateral sclerosis and Huntington’s disease as the most common neurodegenerative diseases. Finally, we proposed some perspective clues for future work.

Myelin oligodendrocyte glycoprotein antibody-associated disease (MOGAD) causes major disability as a consequence of recurrent demyelinating events and neuronal loss. Biomarkers identifying different phenotypes of recurrence or tissue damage might be useful to guide individualized therapy. Herein, we evaluated serum neurofilament light chain (sNfL) as a potential biomarker in both adult and pediatric MOGAD patients. Forty-nine patients with MOGAD (37 adults, 12 children) and 71 healthy controls (HCs) (56 adults, 15 children) were enrolled prospectively from September 2019 to April 2021 at the Third Affiliated Hospital of Sun Yat-sen University and the Children's Hospital, Zhejiang University School of Medicine. sNfL levels were determined using ultrasensitive single-molecule array assay and correlated with clinical parameters. The sNfL levels in MOGAD adults in a relapsed state (median: 31.0 pg/mL) were higher than those in a remission state (8.1 pg/mL, p = 0.001) and in HC adults (10.3 pg/mL, p = 0.004). Similar results were observed in children (relapse: 46.8 pg/mL vs. remission: 13.1 pg/mL, p = 0.001; and vs. HCs: 8.2 pg/mL, p = 0.007) sNfL levels were correlated with recent relapses within 60 days (multivariate: β = 2.02, p = 0.003), seizures (multivariate: β = 2.50, p = 0.021) and brain lesions on magnetic resonance imaging (MRI) of a recent relapse (multivariate: β = 1.72, p = 0.012). Our study showed that sNfL levels are beneficial for identifying recent relapses and seizures and suggest that adult and pediatric MOGAD patients had similar sNfL levels.

Understanding the molecular mechanism behind protein-polyphenol interactions is critical for the application of protein-polyphenol compounds in foods. The purpose of this research was to investigate the non-covalent interaction mechanism between soy protein isolate (SPI) and catechin and its effect on protein conformation. We observed that particle size, ζ-potential, and polyphenol bound equivalents of SPI increased significantly after non-covalent modification with catechin. These changes caused SPI to aggregate and form a network-like structure. Fourier transform infrared spectroscopy (FTIR) indicated that increased catechin concentrations caused SPI to become looser and more disordered as its α-helix and β-sheet transformed into β-turn and random coil. Furthermore, internal structure of SPI was opened and its hydrophobic groups were exposed to a polar environment, which was demonstrated by decreased surface hydrophobicity. Thermodynamic analysis and molecular docking results showed that the main forces present between SPI and catechin were hydrophobic interactions and hydrogen bonds.

Human ALX1 gene (ALX Homeobox 1) is a protein coding gene and gene ontology annotations related to this gene include DNA-binding transcription factor activity and protein heterdimerization activity. It is necessary for survival of forebrain mesenchyme and may be involved in development of cervix. However, the function of the gene has yet to be determined in humans. Here we generated an ALX1 homozygous human embryonic stem cell line (WAe001-A-060) by a CRISPR/Cas9 system. The WAe001-A-060 has a normal undifferentiated morphology and karyotype, pluripotency and three germ layers differentiation potential in vivo.