CRANAD 28 | 1623747-97-6

CRANAD 28 is a specialized chemical compound derived from curcumin, designed primarily as a fluorescent probe for neuroscience research. Known for its strong binding affinity to amyloid-β (Aβ) plaques, CRANAD 28 plays a significant role in the study of Alzheimer’s disease, where these plaques are a major pathological hallmark. Unlike some probes that maintain or increase fluorescence upon binding, CRANAD 28 uniquely decreases in fluorescence intensity when it binds to Aβ. This quenching effect allows researchers to track the presence and quantity of amyloid plaques through fluorescence imaging techniques. Overall, CRANAD 28’s structure and reactivity make it a potent tool in investigating amyloid-related neurodegenerative conditions.

One of the pivotal applications of CRANAD 28 is its use in non-invasive imaging of amyloid plaques in the brain. By exploiting its fluorescence properties, scientists can visualize and quantify the progression of amyloid deposition in vivo. This capability is crucial for early diagnosis and monitoring the progression of Alzheimer’s disease in animal models and potentially in human studies. Through such advanced imaging techniques, researchers can gain insights into disease mechanisms and evaluate the efficacy of therapeutic interventions.

Another significant application of CRANAD 28 is its ability to inhibit Aβ crosslinking induced by copper ions. Copper-induced crosslinking is believed to play a role in the aggregation of Aβ, contributing to the formation of toxic oligomers and fibrils linked to Alzheimer’s pathology. The compound’s inhibitory effect offers a dual function: as both a diagnostic tool and a potential therapeutic agent. Its ability to interfere with the metal ion-mediated aggregation process provides a valuable means to explore therapeutic strategies aimed at mitigating or reversing plaque formation and its associated neurotoxicity.

CRANAD 28’s use extends to studying cerebral amyloid angiopathy (CAA), a condition characterized by the deposition of Aβ within the walls of cerebral vasculature. By binding to Aβ in CAA, the probe supports research into this condition, which is often associated with hemorrhagic strokes and cognitive impairment. Understanding CAA’s pathophysiology is critical, as it contributes to a significant proportion of strokes and dementia cases in the elderly. Thus, CRANAD 28 serves as an instrumental tool in elucidating the complex interactions between amyloid deposits and vascular health.

Furthermore, CRANAD 28 can be utilized in fundamental research to deepen the understanding of the biochemical interactions and pathways involved in Aβ aggregation and toxicity. By providing a means to study these interactions in real-time, it helps scientists decipher the complex cascade of events leading from Aβ monomers to insoluble plaques. This understanding is paramount for developing novel interventions that aim to disrupt these processes at early stages, potentially altering the disease trajectory before significant neuronal damage and cognitive decline occur. Therefore, CRANAD 28 is a versatile compound with applications that span both diagnostic and therapeutic research in neurodegenerative diseases.