The Cocktail Report (sounds really smart around your friends):
As you age, sugars and reactive molecules permanently attach to proteins in the structural scaffolding around your cells, forming advanced glycation end products (AGEs) chemical damage long considered a one-way street
The most common AGE on your proteins is called CML (carboxymethyl-lysine), and it accumulates with age on collagen, arterial walls, and lens tissue; it also activates an inflammatory receptor called RAGE, contributing to the baseline inflammation seen in aging
No natural human enzyme can remove CML, which is exactly why the researchers had to engineer one from scratch, screening over 500 million variants through a process called directed evolution
Applied to elderly human skin tissue sections, CMLase reduced CML staining by more than 55%, bringing levels below those typically found in 31-year-old skin
Applied to elderly arterial tissue, CMLase achieved more than 70% reduction in CML content
This is personally relevant because AGEs accumulate in every person's body regardless of lifestyle. You can optimize sleep, diet, and exercise, but the structural proteins around your cells still collect this chemical damage over decades.
Until now, there was no way to reverse it. The research team started with a bacterial enzyme called a glycine oxidase, chosen because glycine is chemically similar to CML, reasoning that it might have weak accidental activity on the right target.
After screening 16 bacterial homologs and finding one with faint useful activity, they ran five rounds of directed evolution. This technique forces bacteria to evolve the enzyme by making their survival dependent on its performance, so only bacteria harboring an enzyme capable of cutting CML off proteins could grow.
After screening 500 million variants, the final enzyme, CMLase, had 15 amino acid substitutions and two deletions relative to its bacterial ancestor. On a panel of proteins including collagen, hemoglobin, and casein, it reduced CML content by 52% to 97%.
On elderly human arterial tissue, CMLase achieved more than 70% reduction in CML. On elderly human skin sections, it reduced CML staining to below what is typically found in a 31-year-old.
Worth noting: all of this work was done on thin tissue sections and isolated proteins, not in living organisms. The key open question is whether removing CML from living tissue actually silences the RAGE inflammatory receptor and improves tissue function measurably.
The enzyme also originated in bacteria, which raises potential immune response concerns requiring further engineering before any human application. The authors are already working on extending the platform to glucosepane, a dominant cross-link in human tissue that stiffens arteries and skin and has resisted reversal for decades.
Why Should You Care?
For the first time, a chemical aging mark that has accumulated in your structural proteins since childhood can be enzymatically erased. This opens a new class of potential therapies that work not by editing genes or clearing cells, but by repairing the molecular scaffolding that holds tissue together.
1. Trabosh N. et al., "Reversal of protein chemical aging by enzymatic deglycation," Nature Communications, Vol. 17, Article 5926, 2026 — https://doi.org/10.1038/s41467-026-75141-2
2. Sheekey Science Show video explainer, July 26, 2026 — https://youtu.be/fGjWaC5ZnPI
