Study Finds Nattokinase Dissolves 84% of Amyloid Microclots Within 2 Hours In Vitro
A natural enzyme potently degrades the same amyloid microclots recently found in 100% of COVID-19 vaccinated individuals tested.
A recent peer-reviewed study by
Grixti et al, published in the
Journal of Experimental and Clinical Application of Chinese Medicine, used purified recombinant nattokinase and a high-resolution automated microscopy system to observe exactly what happens when the enzyme directly contacts amyloid fibrin(ogen) microclots.
To generate true amyloid microclots, the researchers mixed fibrinogen with LPS, triggered clot formation with thrombin, and labeled the resulting structures with Thioflavin-T — producing the same β-sheet, ThT-positive fibrinaloid clots seen in human Long COVID and post-vaccine samples.
Nattokinase was then added at two concentrations:
14 µg/mL and
28 µg/mL — levels that fall within the range achievable in humans following high-dose oral administration.
At the higher dose (
28 µg/mL), nattokinase reached peak activity at around
2 hours and produced:
- ~84% reduction in total clot number
(Figure 4A: 920 → 150)
- ~52% reduction in total amyloid fluorescent intensity
(Figure 4B: 2500 RU → 1200 RU)
- ~20% reduction in median clot size
(Figure 4C: 15 µm → 12 µm — though this metric underestimates true digestion because the smallest clots disappear first)
At the lower dose (
14 µg/mL), nattokinase still produced substantial, dose-dependent effects:
- ~67% reduction in total clot number
(920 → 300)
- ~20% reduction in total amyloid intensity
(2500 RU → 2000 RU)
- ~7% reduction in median clot size
(15 µm → 14 µm)
In other words:
nattokinase directly digested amyloid fibrin(ogen) structure.
The authors state this explicitly:
We show that recombinant nattokinase is effective at degrading the fibrinaloid microclots in vitro.
This is the strongest biochemical evidence to date that a natural fibrinolytic enzyme can break down the same amyloid microclots now found in the blood of vaccinated individuals and Long COVID patients.
Potent Dual-Activity
Amyloid fibrin microclots are not ordinary clots. They are structurally misfolded, β-sheet amyloid constructs that resist plasmin, resist rtPA, and trap inflammatory proteins in a dense mesh. Their resistance to dissolution means they can persist in circulation, obstruct capillaries, and contribute to a long list of chronic symptoms.
Adding to this, nattokinase has already been
shown in studies to degrade the SARS-CoV-2 spike protein itself (in-vitro) —the same protein that drives amyloid transformation of fibrinogen and accelerates the formation of fibrinaloid microclots. This was one of the primary reasons nattokinase was incorporated into
McCullough Protocol Base Spike Detoxification:
https://pmc.ncbi.nlm.nih.gov/articles/PMC10663976/
This dual activity is significant: nattokinase appears to be able to break down both the trigger (spike)
and the pathological result (amyloid microclots). No pharmaceutical thrombolytic therapy has demonstrated this combined effect.
This makes nattokinase one of the few agents with a plausible mechanism to reduce amyloid clot burden without requiring invasive procedures, mechanical devices, or hospital-grade thrombolytics.
Secondary Evidence: Mechanical Clot Destruction via Ultrasound
Alongside this nattokinase study, another recent paper by
Rasouli et al demonstrated that amyloid microclots can also be physically fragmented using
low-frequency ultrasound,
gas microbubbles, and
rtPA in a microfluidic vein model. In the strongest condition — low-frequency ultrasound combined with microbubbles and rtPA — large amyloid microclots (>30 µm) were reduced from ~550 to ~20 (Figure 5F), representing a
>90% reduction. This demonstrates that cavitation-enhanced ultrasound can physically shatter nearly all large amyloid microclots in a controlled microfluidic model.
pubmed.ncbi.nlm.nih.gov
