Enzyme reduces a form of protein damage in human tissue
Overnight exposure reduced an age-linked protein modification by 45% in lens proteins from a 64-year-old donor, compared with untreated samples.
Limit: Lens damage reduction differed by assay: 78% by antibody versus 45% by chemical analysis
Stake: An author holds a patent on this work.
Edited by Boris Djordjevic · AgingResearch.News
Researchers tested an engineered enzyme on lens proteins from a 64-year-old human donor and on skin and artery tissue from elderly donors in laboratory experiments. The enzyme, CMLase, targets carboxymethyl-lysine, a chemical modification that accumulates on long-lived proteins with age. Researchers developed it by screening more than 500 million enzyme variants.
After overnight exposure to 5 micromolar CMLase, lens proteins contained 45% less of the modification than untreated samples, measured by chemical analysis. In artery and skin sections, the same dose and duration reduced staining for the modification by more than 70% and more than 55%, respectively, compared with an inactive enzyme. Experiments on model proteins also showed that CMLase could remove the modification and restore lysine, a protein building block.
Why it matters
Chemical damage accumulates in long-lived proteins during aging. The authors propose enzyme engineering as a platform for repairing age-related molecular damage.
Caveats
These experiments tested donated samples in the laboratory, not whether the enzyme improved health in living people. An antibody-based lens assay indicated a 78% reduction, compared with 45% by chemical analysis.
- Cmlase
- Resources: datasets, atlases and tools
- AGER
- Advanced glycation end products
- Nε-(carboxymethyl)lysine
- Humans
The paper
Reversal of protein chemical aging by enzymatic deglycation
Revel Pharmaceuticals, Inc. (United States)
Nature Communications, Jul 14, 2026, Open access
