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aggregation properties of a therapeutic peptide for rheumatoid arthritis:A spectroscopic and molecular dynamics study

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ChemPhysMater 2022年第1期1卷 62-70页

作者： Rita Cimino Marco Savioli Noemi Ferrante Carrante Ernesto Placidi Hilda Garay-Perez Matilde López-Abad Alexis Musacchio Lasa Maria Del Carmen Domínguez-Horta Emanuela Gatto Francesca Cavalieri Gianfranco Bocchinfuso Mariano Venanzi PEPSA-LAB Department of Chemical Sciences and TechnologyUniversity of Rome Tor VergataVia della Ricerca Scientifica 100133RomeItaly Department of Physics University of Rome‘Sapienza’P.le A.Moro 500185 RomeItaly Centre for Genetic Engineering and Biotechnology PO Box 616210600HavanaCuba School of Science RMIT UniversityMelbourneVIC 3001Australia

The biological properties of therapeutic peptides,such as their pharmacokinetics and pharmacodynamics,are correlated with their structure and aggregation ***,we studied the aggregation properties of a therapeutic peptide(CIGB-814),currently in phase 2 clinical trial,for the treatment of rheumatoid arthritis over a wide range of concentrations(μM-mM).We applied spectroscopic techniques(fluorescence,circular dichro-ism,resonance,and dynamic light scattering),atomic force microscopy,and molecular dynamics simulations to determine the aggregation mechanism of *** found that the hierarchical aggregation of CIGB-814 at micromolar concentrations was initiated by the formation of peptide ***,the peptide oligomers trigger the nucleation and growth of peptide nanostructures(cac=123μM),ultimately leading to the fibrillization of CIGB-814(cac’=508μM).These results pave the way for a deeper understanding of the CIGB-814 therapeutic activity and may give important insights on its pharmacokinetics.

关键词： Molecular dynamics of peptide oligomers peptide aggregation peptide fibrils peptide nanostructures Therapeutic peptides Treatment of rheumatoid arthritis

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Flavones in pomelo peel resist fibril formation of human islet amyloid polypeptide

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Chinese Herbal Medicines 2025年第1期17卷 166-177页

作者： Cuiyun Gao Zhiruo Wan Yan Liu Yuting Meng Xu Chen Xiaohan Tang Lingyu Hang Hailong Yuan Department of Pharmacy Air Force Medical Center Air Force Medical University

Objective:Exploring the formation and aggregation of human islet amyloid polypeptide(hIAPP)(amylin)fibers is significant for promoting the prevention and treatment of type II diabetes mellitus(T2DM).Flavones in pomelo peel have visible biological activity in the anti-diabetes *** present study aimed to investigate the effects of five flavones [naringin(NRG),narirutin(NRR),nobiletin(NOB),sinensetin(SIN),and neohesperidin(NHP)] in pomelo peel on peptide aggregation and explore its possible *** cell viability of flavones against peptide aggregation was also ***:The thioflavin T(ThT) assay and transmission electron microscopy(TEM) were used for evaluating the inhibition and disaggregation of flavones on peptide *** interaction mechanism was analyzed by endogenous fluorescence,molecular dynamics(MD) simulations,ultraviolet spectroscopy(UV) and isothermal titration calorimetry(ITC) *** 3-[4,5-dimethylthiazol-2-y l]-2,5-diphenyl tetrazolium bromide(MTT) and immune assays were performed to characterize the cell viability of flavones against peptide ***:The five flavones showed a decrease in fluorescence intensity,fiber number and size under incubation with different molar ratios of *** compounds can bind to the aromatic tyrosine(Tyr)residueTyr 37,resulting in the intrinsic fluorescence quenching of the *** flavones can form hydrogen bonds with hIAPP,which is likely to be based on their phenolic hydroxyl *** showed strong binding affinity with *** reaction system of NRG and NRR observed an exothermic reaction,and the others were endothermic *** absorption peaks of the compounds with hIAPP changed and showed hypochromic effects,indicating that there may be π-π stacking *** noticeably increased the cell viability in the presence of amyloid peptides and reduced the absorption intensity induced by peptide ***:A total of five flav

关键词： flavones human islet amyloid polypeptide inhibition interaction pomelo peel peptide aggregation

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Significance of native PLGA nanoparticles in the treatment of Alzheimer’s disease pathology

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Bioactive Materials 2022年第11期7卷 506-525页

作者： Bibin Anand Qi Wu Maryam Nakhaei-Nejad Govindarajan Karthivashan Lyudmyla Dorosh Sara Amidian Abhishek Dahal Xiuju Li Maria Stepanova Holger Wille Fabrizio Giuliani Satyabrata Kar Department of Medicine(Neurology) University of AlbertaEdmontonAlbertaT6G 2M8Canada Centre for Prions and Protein Folding Diseases University of AlbertaEdmontonAlbertaT6G 2M8Canada Department of Electrical and Computer Engineering University of AlbertaEdmontonAlbertaT6G 2M8Canada Department of Biochemistry University of AlbertaEdmontonAlbertaT6G 2M8Canada Neuroscience and Mental Health Institute University of AlbertaEdmontonAlbertaT6G 2M8Canada

Alzheimer’s disease (AD) is believed to be triggered by increased levels/aggregation of β-amyloid (Aβ) peptides. At present, there is no effective disease-modifying treatment for AD. Here, we evaluated the therapeutic potential of FDA-approved native poly(D,L-lactide-co-glycolide) (PLGA) nanoparticles on Aβ aggregation and in cellular/ animal models of AD. Our results showed that native PLGA can not only suppress the spontaneous aggregation but can also trigger disassembly of preformed Aβ aggregates. Spectroscopic studies, molecular dynamics simu-lations and biochemical analyses revealed that PLGA, by interacting with the hydrophobic domain of Aβ1-42, prevents a conformational shift towards the β-sheet structure, thus precluding the formation and/or triggering disassembly of Aβ aggregates. PLGA-treated Aβ samples can enhance neuronal viability by reducing phosphor-ylation of tau protein and its associated signaling mechanisms. Administration of PLGA can interact with Aβ aggregates and attenuate memory deficits as well as Aβ levels/deposits in the 5xFAD mouse model of AD. PLGA can also protect iPSC-derived neurons from AD patients against Aβ toxicity by decreasing tau phosphorylation. These findings provide unambiguous evidence that native PLGA, by targeting different facets of the Aβ axis, can have beneficial effects in mouse neurons/animal models as well as on iPSC-derived AD neurons - thus signifying its unique therapeutic potential in the treatment of AD pathology.

关键词： Alzheimer’s disease β-amyloid Nanoparticles Neuroprotection peptide aggregation

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