Could Somatostatin be the Elusive Alzheimer’s Disease Drug?
AMYLOID-β (Aβ) is the main component of the amyloid aggregates found in the brains of individuals with Alzheimer’s disease. Many drugs in clinical trials have attempted to tackle Alzheimer’s disease by targeting Aβ aggregates, with limited success. However, binding to the smaller aggregates, which are considered the most toxic to neurons, has not been possible so far, but a new study has shown that somatostatin can achieve this, providing hope for this approach to be successful.
In a recent study, researchers at Uppsala University, Uppsala, Sweden, have developed a novel treatment method in mice in which the peptide somatostatin degrades the building blocks from which the aggregates form, preventing the formation of all types of aggregates. Somatostatin has been shown to catalyse the body’s own degradation of Aβ; however, utilising somatostatin as a drug has not been possible because of its extremely short half-life in the blood and its inability to cross the blood–brain barrier to target the aggregates in the brain.
In their attempt to use somatostatin as a treatment, the researchers “fused it to a brain transport protein, which allows the somatostatin to enter the brain. This has proved very effective. When we used the transport protein, we also saw that the time that the somatostatin remained in the brain increased to several days” stated Fadi Rofo, doctoral student, Uppsala University. Results revealed the greatest effects in the hippocampus, the part of the brain responsible for memory formation and the first to be affected by Alzheimer’s disease.
The current study was conducted in mice, but the researchers are optimistic that somatostatin would exert similar effects in humans and prove to be more effective than current treatment options. Assistant Prof Greta Hultqvist from the same institute positively stated: “Our hope is that this method will be able to act in a very targeted way and have few side effects, which have been a problem in other studies.”