Entity

Time filter

Source Type

Laval, Canada

Aisen P.S.,University of California at San Diego | Gauthier S.,ll Center for Studies in Aging | Ferris S.H.,New York University | Ferris S.H.,Nathan Kline Institute | And 9 more authors.
Archives of Medical Science | Year: 2011

Introduction: The aim of the study was to assess the clinical efficacy, safety, and disease-modification effects of tramiprosate (homotaurine, ALZHEMED™) in mild-to-moderate Alzheimer's disease (AD). Material and methods: Double-blind, placebo-controlled, randomized trial in 67 clinical centres across North America. Patients aged ≥ 50 years, with mild-to-moderate AD (Mini-Mental State Examination score between 16 and 26) and on stable doses of cholinesterase inhibitors, alone or with memantine. Intervention: 78-week treatment with placebo, tramiprosate 100 mg or tramiprosate 150 mg BID. Measurements: Alzheimer Disease Assessment Scale - cognitive subscale (ADAS-cog) and Clinical Dementia Rating - Sum of Boxes (CDR-SB) assessments were performed at baseline and every 13 weeks. Baseline and 78-week magnetic resonance imaging (MRI) hippocampus volume (HV) measurements were conducted in a subgroup of patients. Results: A total of 1,052 patients were enrolled and 790 (75.1%) completed the 78-week trial. Patient discontinuation and reasons for withdrawal were similar across groups. Planned analyses did not reveal statistically significant between-group differences. Lack of adequate statistical validity of the planned analysis models led to the development of revised predictive models. These adjusted models showed a trend toward a treatment effect for ADAS-cog (P = 0.098) and indicated significantly less HV loss for tramiprosate 100 mg (P = 0.035) and 150 mg (P = 0.009) compared to placebo. The incidence of adverse events was similar across treatment groups. Conclusions: The primary planned analyses did not show a significant treatment effect, but were confounded by unexplained variance. Post-hoc analyses showed a significant treatment-related reduction in HV loss. However, there was only a trend towards slowing of decline on the ADAS-cog and no slowing of decline on the CDR-SB. These results must be interpreted in consideration of the limitations of clinical and disease-modification outcome measures and their relationship, the heterogeneity of the disease and the impact of confounding demographic and clinical variables. Copyright © 2011 Termedia & Banach. Source


Trademark
BELLUS Health Inc. and Innodia Inc. | Date: 2005-11-11

Pharmaceuticals and nutraceuticals for the prevention and treatment of metabolic diseases, namely diabetes including microvascular and macrovascular complications, and obesity. Research and development of pharmaceuticals and nutraceuticals for the prevention and treatment of metabolic diseases, namely diabetes including microvascular and macrovascular complications, and obesity.


Patent
BELLUS Health Inc. | Date: 2011-09-20

Methods, compounds, pharmaceutical compositions and kits are described for treating or preventing amyloid-related disease.


The invention relates to methods, compounds, and compositions for delivering 1,3-propanedisulfonic acid (1,3PDS) in a subject, preferably a human subject. The invention encompasses compounds that will yield or generate 1,3PDS, either in vitro or in vivo. The invention also relates to sulfonate ester prodrugs of 1,3PDS as well as Gemini dimmers and oligomers of 1,3PDS for the prevention or treatment of associated diseases and conditions.


Martineau E.,University of Ottawa | Martineau E.,BELLUS Health Inc. | de Guzman J.M.,BELLUS Health Inc. | Rodionova L.,BELLUS Health Inc. | And 3 more authors.
Journal of the American Society for Mass Spectrometry | Year: 2010

This paper describes an efficient and reproducible screening method for identifying low molecular weight compounds that bind to amyloid β peptides (Aβ) peptides using electrospray ionization mass spectrometry (ESI-MS). Low molecular weight compounds capable of interacting with soluble Aβ may be able to modulate/inhibit the Aβ aggregation process and serve as potential disease-modifying agents for AD. The present approach was used to rank the binding affinity of a library of compounds to Aβ1-40 peptide. The results obtained show that low molecular weight compounds bind similarly to Aβ1-42, Aβ1-40, as well as Aβ1-28 peptides and they underline the critical role of Aβ peptide charge motif in binding at physiological pH. Finally, some elements of structure-activity relationship (SAR) involved in the binding affinity of homotaurine to soluble Aβ peptides are discussed. © 2010. Source

Discover hidden collaborations