N-Acetyl Cysteine (NAC) for Protein Folding Support
NAC supports glutathione-dependent redox control of protein handling, but proteostasis benefits are unproven.
Overview
Verdict
How It Works
Dosing & Protocol
Typical dose
- Recommended dose
- 600-1200mg/day
- Expected timeframe
- Unknown
Protocol
- form
- Not applicable
- duration
- Not applicable
- co factor
- Evidence is insufficient. There is a genuine biochemical connection - correct protein folding depends on disulfide bond formation in the endoplasmic reticulum, and the glutathione redox couple helps set the thiol-disulfide balance that protein disulfide isomerase uses to form and reshuffle those bonds. NAC raises glutathione, so a link is arguable in principle. But no human trial has measured protein folding, endoplasmic reticulum stress markers or the unfolded protein response as an outcome of NAC supplementation, and the evidence that exists is cell culture and animal work. Shifting the cytosolic redox state more reducing is also not straightforwardly beneficial, since disulfide bond formation requires oxidising conditions in the ER - more antioxidant is not obviously better here.
- titration
- Not applicable
- starting dose
- Not applicable as an established intervention
Evidence
What the studies say
N-acetylcysteine, oxidative stress and protein misfolding: a systematic review of clinical evidence
Tenorio MCDS, Graciliano NG, Moura FA +2 more
NAC reliably raised glutathione and reduced markers of protein oxidation and carbonylation
Safety
Caveats
Nausea is common. Not a substitute for exercise or sleep.
Less likely to help if
Medical Disclaimer
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Individual results may vary. The statements on this website have not been evaluated by the Food and Drug Administration. Products and information are not intended to diagnose, treat, cure, or prevent any disease.