Revel Pharmaceuticals reported a proof of concept enzyme that removed the aging-related glycation marker CML from highly glycated aorta tissue taken from a 75-year-old human donor.
CML builds up because no natural human enzyme reverses the modification, and the damage is linked to tissue stiffening and inflammation in aging and diabetes.
Directed evolution produced the enzyme after bacterial glycine oxidases showed little activity against CML embedded in peptides; the final version selectively cleaved CML without hitting other amino acids or glycation products.
Low activity remains the main hurdle, and Revel said it needs stronger potency before moving into animal studies for diabetic retinopathy.
The work, published in Nature Communications, suggests advanced glycation end products may be chemically reversible rather than permanently accumulating in long-lived proteins.