The efficiency, safety, and clinical potential of semorinemab in the treatment of Alzheimer's disease

Abstract

Alzheimer's disease (AD) has become a global high-impact disease. Research from the last century to the present day has not revealed the underlying pathological mechanisms of its development. The most authoritative hypotheses about the cause of AD have been proposed in relation to tau and Aβ proteins. Drugs used in clinical practice today for the treatment of AD provide only relative symptomatic relief. Using tau P301L mutant mice, it was demonstrated that in AD brain structures, tau proteins form tangles that produce toxins that affect normal neuronal function. These experiments confirm the link and interaction between Aβ and tau proteins, highlighting the importance and potential of interventions targeting the aggregation of both proteins in the development of new therapeutic strategies for AD. The aim of this paper is to study a human monoclonal antibody for semorinemab, using tau P301L-Tg mice and Crab monkeys as experimental models, and to investigate the therapeutic effect of semorinemab on AD in the early stages is more significant results, and has a high safety and stability. However, semorinemab did not show significant therapeutic results in mid-stage AD clinical trials. Phase II studies of semorinemab in AD are ongoing.