Alzheimer’s disease (AD) is an incurable neurodegenerative disease that is the leading cause of dementia worldwide [1]. A key characteristic of AD is the deposition of plaques formed by the amyloid-β (Aβ) peptide. However, despite extensive development efforts, anti-Aβ therapies have shown very modest clinical impact on cognitive decline [2]. Therefore, there remains an urgent and unmet need for novel therapeutics that target different pathological mechanisms in AD. The voltage-gated potassium channel KV1.3 is upregulated in pro-inflammatory microglia that mediate neuroinflammation in AD. KV1.3 blockade has been shown to be therapeutically beneficial in animal models of AD by shifting microglia away from a pro-inflammatory phenotype, reducing neuroinflammation, and improving cognitive function [3].
HsTX1[R14A] is a potent peptide blocker of KV1.3 (IC50 45 pM) that is highly selective (>2000-fold) for KV1.3 over closely-related KV1 channels [4]. We have shown that HsTX1[R14A] reduces microglial activation in vitro and in an animal model of neuroinflammation [5,6]. Compared to other peptide inhibitors of KV1.3, HsTX1[R14A] is more potent and selective for KV1.3, simpler and cheaper to make, and more stable chemically and proteolytically. It thus represents a highly promising molecule for AD therapeutic development.
Our recently published data show that unmodified HsTX1[R14A] at 1 mg/kg is able to improve cognitive function in a mouse model of sporadic AD (the most common form of AD) [7]. Given its size and polarity, HsTX1[R14A] likely accesses the brain as a consequence of blood-brain barrier (BBB) disruption in this model. I will describe our current efforts towards improving the brain uptake of HsTX1[R14A], which will decrease the dose of peptide required and enable treatment before the disease progresses to a stage where the BBB is compromised. This work will position HsTX1[R14A] as a novel brain-penetrant drug lead for further clinical development.