A new study demonstrates that factors present in aged blood can accelerate the accumulation of amyloid proteins and influence behavior in an experimental mouse model of Alzheimer's.

Researchers have developed a new tool, FibrilPaint combined with the FibrilRuler test, that allows scientists to directly measure the length of toxic Tau amyloid fibrils in tiny fluid samples, from the earliest aggregation stages to mature fibrils and even at very low concentrations. Because Tau fibrils are tightly linked to Alzheimer’s and other dementias, yet have been extremely difficult to quantify in solution, this “molecular ruler” represents a major advance. It works in complex, patient-derived samples and selectively recognizes amyloid fibrils from several neurodegenerative diseases, enabling far more precise studies of how these fibrils grow, break, and respond to potential drugs and, in the longer term, could underpin new diagnostic tools or biomarkers that track disease progression or treatment response via fibril length.

Alzheimer’s disease (AD) imposes a substantial clinical and societal burden, yet currently approved symptomatic therapies do not modify the underlying disease biology. Recently, three anti-amyloid monoclonal antibodies (aducanumab, lecanemab, and donanemab) have demonstrated robust amyloid clearance. Their clinical effects are statistically significant but modest, underscoring the need for broader, biologically informed strategies. Guided by the 2024 Alzheimer’s association ATNIVS biomarker framework, a team form Xuanwu Hospital, Capital Medical University synthesizes disease-modifying therapies (DMTs) targeting amyloid (A), tau (T), neurodegeneration (N), inflammation (I), vascular injury (V), and α-synuclein (S), summarizing the candidate therapies for each target, explain the mechanisms of action and pivotal clinical trial results. The review is currently published on the journal Medicine Plus.