Read our selection of the most exciting research papers recently published.


Diagnostic Utility of Selected Serum Dementia Biomarkers: Amyloid β-40, Amyloid β-42, Tau Protein, and YKL-40: A Review

This article reviews several papers on the concentrations of Aβ40, Aβ42, tau protein and YKL-40 and found that the results between the cognitive disorders group and control group for the Aβ40 and Aβ42 groups were incoherent. However, they found that in the patients with AD, there was increased tau protein concentration. They also found that increased YKL-40 concentration was significant in those diagnosed with mild cognitive impairment which can progress to AD. The authors also found the ratio of t-tau/Aβ42 a significant biomarker in those with cognitive disorders such as AD.

Research Target: Aβ40, Aβ42, tau,

Read the full article in Journal of Clinical Medicine, October 2020.


Relation between alpha‐synuclein and core CSF biomarkers in Alzheimer's disease

It is hypothesized that amyloid beta, tau protein and alpha synuclein are involved in Alzheimer’s disease and that these proteins all lead to the accumulation of one another. In this study, the authors did a follow-up of patients diagnosed with mild cognitive impairment and while some of them remained at this stage, others progressed to Alzheimer’s disease or another neurodegenerative disease. The authors measured for amyloid beta levels, tau protein and alpha synuclein (α-syn) with the human ELISA kits.

The authors found that the α-syn levels significantly correlated with tau protein in patients with AD. The tau proteins were significantly related to AD. Due to the exclusive correlation between α-syn and tau, the authors suggest α-syn as a protein involved in the pathology of AD.

Research Target: α-syn, tau,

Read the full article in Alzheimer's Association, December 2020.

Preventative therapy for Alzheimer’s disease (AD)

Anogen is the first company to develop the concept of preventative Pre-AD treatment in the world.

Since 2009, we have been developing antibody-based therapies for AD, and generated over 70 monoclonal antibodies (mAbs) against various amyloid β (Aβ) peptides. Three of these mAbs (3F5, 6C8, and 1H3) have shown efficacy in prevention of the progression of AD in mouse models. We have also developed an ELISA kit for quantitative measurement of Aβ42, a major causative factor of AD. Our pre-AD project is the first attempt to use anti-Aβ42 mAbs for AD prevention and treatment via an intranasal route.

After nine years of research on anti-Aβ42 antibodies, we recognized that administering anti-Aβ42 mAbs after pathological changes in the brain had already occurred would not significantly reduce plaque numbers in AD mouse brain. Our new preclinical study (pre-AD treatment) has focused on preventing the aggregation of Aβ42 in mouse brain since early 2016.

Antibodies targeting the N-terminus of Aβ42 were further studied in collaboration with scientists at NIH in USA and the Army Medical University in China. The antibodies reduced plaque numbers and improved cognition of double transgenic AD mice (APP/PS1). The study showed that after 3F5 mAb treatment, the level of Aβ42 in the brain tissue was significantly decreased. The result of the study was published in the journal PLoS ONE in June 2017.

Our Pre-AD project delivers anti-Aβ42 mAbs to the brain via an intranasal route, which is direct and non-invasive that bypasses the blood-brain barrier (BBB). Intranasal delivery to the brain increases drug concentration in the brain, reduces systemic side effect, is painless and patient-friendly, and improves drug performance.

In addition to Aβ42, we also developed antibodies against phosphorylated tau proteins that may prevent neurofibrillary tangle formation. We also recognized that inflammatory reactions are linked to amyloid plaques and neurofibrillary tangles, thus have designed cocktail therapies using antibodies against Aβ42 and multiple human cytokines to increase the effectiveness of antibody therapy in preventing AD.


Y Zhang et al., Amyloid-β induces hepatic insulin resistance in vivo via JAK2. Diabetes (2013) 62, 4:1159-1166.

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