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Unveiling the inhibition mechanism of host-defense peptide cathelicidin LL-37 on the amyloid aggregation of the human islet amyloid polypeptide.
Nanoscale
January 2025
Department of Engineering Mechanics, Hohai University, Nanjing 211100, P.R. China.
The aberrant aggregation of the human islet amyloid polypeptide (hIAPP) is a hallmark of type II diabetes. LL37, the only cathelicidin host-defense peptide in humans, plays essential roles in antimicrobial and immunomodulatory activities. Mounting evidence indicates that LL37 can inhibit the amyloid aggregation of hIAPP, suggesting possible interplays between infections and amyloid diseases while the mechanism remains unclear.
View Article and Find Full Text PDFRole of Copper and Zinc Ions in the Hydrolytic Degradation of Neurodegeneration-Related Peptides.
Molecules
January 2025
Dipartimento di Chimica, Università di Pavia, Via Taramelli 12, 27100 Pavia, Italy.
Spontaneous cleavage reactions normally occur in vivo on amino acid peptide backbones, leading to fragmentation products that can have different physiological roles and toxicity, particularly when the substrate of the hydrolytic processes are neuronal peptides and proteins highly related to neurodegeneration. We report a hydrolytic study performed with the HPLC-MS technique at different temperatures (4 °C and 37 °C) on peptide fragments of different neuronal proteins (amyloid-β, tau, and α-synuclein) in physiological conditions in the presence of Cu and Zn ions, two metal ions found at millimolar concentrations in amyloid plaques. The coordination of these metal ions with these peptides significantly protects their backbones toward hydrolytic degradation, preserving the entire sequences over two weeks in solution, while the free peptides in the same buffer are fully fragmented after the same or even shorter incubation period.
View Article and Find Full Text PDFmiR-32533 Reduces Cognitive Impairment and Amyloid-β Overload by Targeting CREB5-Mediated Signaling Pathways in Alzheimer's Disease.
Adv Sci (Weinh)
January 2025
Institute of Medicinal Biotechnology, Peking Union Medical College and Chinese Academy of Medical Sciences, Beijing, 100050, P. R. China.
MicroRNAs (miRNAs) are associated with amyloid-β (Aβ) dysmetabolism, a pivotal factor in the pathogenesis of Alzheimer's disease (AD). This study unveiled a novel miRNA, microRNA-32533 (miR-32533), featuring a distinctive base sequence identified through RNA sequencing of the APPswe/PSEN1dE9 (APP/PS1) mouse brain. Its role and underlying mechanisms were subsequently explored.
View Article and Find Full Text PDFα-Synuclein fibrils enhance HIV-1 infection of human T cells, macrophages and microglia.
Nat Commun
January 2025
Institute of Molecular Virology, Ulm University Medical Center, 89081, Ulm, Germany.
HIV-associated neurocognitive disorders (HAND) and viral reservoirs in the brain remain a significant challenge. Despite their importance, the mechanisms allowing HIV-1 entry and replication in the central nervous system (CNS) are poorly understood. Here, we show that α-synuclein and (to a lesser extent) Aβ fibrils associated with neurological diseases enhance HIV-1 entry and replication in human T cells, macrophages, and microglia.
View Article and Find Full Text PDFMulti-Targeting Macrocyclic Peptides as Nanomolar Inhibitors of Self- and Cross-Seeded Amyloid Self-Assembly of α-Synuclein.
Angew Chem Int Ed Engl
January 2025
Technische Universität München, Division of Peptide Biochemistry, Emil-Erlenmeyer-Forum 5, 85354, Freising, GERMANY.
Amyloid self-assembly of α-synuclein (αSyn) is linked to the pathogenesis of Parkinson's disease (PD). Type 2 diabetes (T2D) has recently emerged as a risk factor for PD. Cross-interactions between their amyloidogenic proteins may act as molecular links.
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