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The structure of FCGBP is formed as a disulfide-mediated homodimer between its C-terminal domains.
FEBS J
January 2025
Department of Medical Biochemistry and Cell Biology, Institute of Biomedicine, University of Gothenburg, Sweden.
Mucus in the colon is crucial for intestinal homeostasis by forming a barrier that separates microbes from the epithelium. This is achieved by the structural arrangement of the major mucus proteins, such as MUC2 and FCGBP, both of which are comprised of several von Willebrand D domains (vWD) and assemblies. Numerous disulfide bonds stabilise these domains, and intermolecular bonds generate multimers of MUC2.
View Article and Find Full Text PDFDbi1 is an oxidoreductase and an assembly chaperone for mitochondrial inner membrane proteins.
EMBO Rep
January 2025
LMU Munich, Biozentrum-Cell Biology, 82152, Planegg-Martinsried, Germany.
Import and assembly of mitochondrial proteins into multimeric complexes are essential for cellular function. Yet, many steps of these processes and the proteins involved remain unknown. Here, we identify a novel pathway for disulfide bond formation and assembly of mitochondrial inner membrane (IM) proteins.
View Article and Find Full Text PDFMRI guided copper deprivator activated immune responses and suppressed angiogenesis for enhanced antitumor immunotherapy.
Theranostics
January 2025
School of Pharmacy, Shandong Technology Innovation Center of Molecular Targeting and Intelligent Diagnosis and Treatment, Binzhou Medical University, Yantai 264003, China.
Copper plays an important role in the regulation of PD-L1, suggesting that reducing copper levels within tumors may enhance anti-cancer immunotherapy. Tumor microenvironment responsive copper nanodeprivator (TMECN) was developed for enhancing immunotherapy of tumor via the cross-link of mercaptopolyglycol bipyridine and dimercaptosuccinic acid modifying FePt nanoalloy using the disulfide bond. Upon entering tumor cells, the disulfide bond in TMECN is cleaved by the overexpressed glutathione, exposing abundance of sulfhydryl groups.
View Article and Find Full Text PDFPositive Charge-Concentrated Dimeric Lipopeptides with Enhanced Protease Resistance: A Potential Solution for Systemic Bacterial Infections.
J Med Chem
January 2025
College of Animal Science and Technology, Northeast Agricultural University, Harbin 150030, People's Republic of China.
Antimicrobial peptides (AMPs) show potential as antibiotic alternatives for bacterial infections; nevertheless, the susceptibility to proteases limits their broader utilization. This study developed engineered lipopeptides using antienzymolysis modifications and cysteine (Cys)-dimerization strategy. As the key parameters for the functioning of AMPs, hydrophobicity and positive charges were concentrated within the peptide sequence by adjusting the intermolecular disulfide bond placement to study their distribution effects.
View Article and Find Full Text PDFAn Imaged Capillary Isoelectric Focusing Separation of the Linear and Cyclic Variants of a Mimotope of the Cancer-Related CD20 Antigen-Validation and Statistical Evaluation.
J Sep Sci
January 2025
Department of Biosciences and Medical Biology, University of Salzburg, Salzburg, Austria.
Imaged capillary isoelectric focusing was successfully applied for separating an in-house synthesized closely related peptide pair, that is, a linear 12-mer (Rp5-L) and its cyclic 15-mer variant (Rp5-C). Rp5-L represents a mimotope, that is, an epitope mimicking peptide, of the CD20 antigen, which is over-expressed in B-cell-related tumors. Peptide identity-including the successful disulfide bond formation in Rp5-C-was confirmed with matrix-assisted laser desorption ionization-time of flight mass spectrometry.
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