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Randomised, Double-blind, Placebo-controlled Study to Assess Safety and Efficacy of PRI-002 in Patients With MCI to Mild Dementia Due to Alzheimer's Disease (AD) (PRImus-AD)

Alzheimer's disease (AD) is the most common form of dementia. In the brains of people with AD, certain small substances stick together. This leads to changes in thinking and behaviour. The company PRInnovation is developing a new treatment for Alzheimer's disease, called PRI-002. It is thought that PRI-002 can cut the sticked substances back into small pieces. That would reduce the effects of Alzheimer's disease. In the current study the investigators examine whether PRI-002 is safe and effective in participants with mild cognitive impairment (MCI) or mild dementia due to AD.

开始日期2023-12-01

申办/合作机构

Prinnovation GmbH

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100 项与 Priavoid GmbH 相关的临床结果

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0 项与 Priavoid GmbH 相关的专利（医药）

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4

项与 Priavoid GmbH 相关的文献（医药）

2023-02-17·ACS Chemical Biology

Discovery of All-d-Peptide Inhibitors of SARS-CoV-2 3C-like Protease

作者: Lakomek, Nils A. ; Santur, Karoline ; Willbold, Dieter ; Gering, Ian ; Strodel, Birgit ; Mohrlüder, Jeannine ; Scharbert, Lara ; Sevenich, Marc ; Eberle, Raphael J. ; Coronado, Mônika A.

2022-07-13·Journal of Virology

A So-Far Overlooked Secondary Conformation State in the Binding Mode of SARS-CoV-2 Spike Protein to Human ACE2 and Its Conversion Rate Are Crucial for Estimating Infectivity Efficacy of the Underlying Virus Variant

Article

作者: Sevenich, Marc ; Gering, Ian ; van den Heuvel, Joop ; Mohrlüder, Jeannine ; Willbold, Dieter

The current SARS-CoV-2 pandemic is characterized by the high infectivity of SARS-CoV-2 and its derived variants of concern (VOCs). It has been widely assumed that the reason for its increased cell entry compared with SARS-CoV (2002) is due to alterations in the viral spike protein, where single amino acid residue substitutions can increase affinity for hACE2.

Biomolecules3区 · 生物学

Alpha-Synuclein-Specific Naturally Occurring Antibodies Inhibit Aggregation In Vitro and In Vivo

3区 · 生物学

ArticleOA

作者: Schulz, Jörg B. ; Willbold, Dieter ; Kupreichyk, Tatsiana ; Hoyer, Wolfgang ; Braczynski, Anne K. ; Stoldt, Matthias ; Agerschou, Emil D. ; Gering, Ian ; Kronimus, Yannick ; Habib, Pardes ; Bach, Jan-Philipp ; Falkenburger, Björn H. ; Sevenich, Marc

Parkinson’s disease (PD) is associated with motor and non-motor symptoms and characterized by aggregates of alpha-synuclein (αSyn). Naturally occurring antibodies (nAbs) are part of the innate immune system, produced without prior contact to their specific antigen, and polyreactive. The abundance of nAbs against αSyn is altered in patients with PD. In this work, we biophysically characterized nAbs against αSyn (nAbs-αSyn) and determined their biological effects. nAbs-αSyn were isolated from commercial intravenous immunoglobulins using column affinity purification. Biophysical properties were characterized using a battery of established in vitro assays. Biological effects were characterized in HEK293T cells transiently transfected with fluorescently tagged αSyn. Specific binding of nAbs-αSyn to monomeric αSyn was demonstrated by Dot blot, ELISA, and Surface Plasmon Resonance. nAbs-αSyn did not affect viability of HEK293T cells as reported by Cell Titer Blue and LDH Assays. nAbs-αSyn inhibited fibrillation of αSyn reported by the Thioflavin T aggregation assay. Altered fibril formation was confirmed with atomic force microscopy. In cells transfected with EGFP-tagged αSyn we observed reduced formation of aggresomes, perinuclear accumulations of αSyn aggregates. The results demonstrate that serum of healthy individuals contains nAbs that specifically bind αSyn and inhibit aggregation of αSyn in vitro. The addition of nAbs-αSyn to cultured cells affects intracellular αSyn aggregates. These findings help understanding the role of the innate immune systems for the pathogenesis of PD and suggest that systemic αSyn binding agents could potentially affect neuronal αSyn pathology.

100 项与 Priavoid GmbH 相关的药物交易

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管线布局中药物为当前组织机构及其子机构作为药物机构进行统计，早期临床1期并入临床1期，临床1/2期并入临床2期，临床2/3期并入临床3期

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药物(靶点)	适应症	全球最高研发状态

PRI-002 ( APP x N-type calcium channel )	阿尔茨海默症更多	临床2期
Fol-PRI-002 ( APP x TYMS )	阿尔茨海默症更多	临床1期
PRI-200 ( TAU )	阿尔茨海默症更多	临床前
PRI-004	神经痛更多	临床前
PRI-100 ( α-synuclein )	家族性1型帕金森病更多	临床前