Resurrected 160-Million-Year-Old Lactoferrin Peptides Outperform Some Modern Versions Against Superbugs
A University of Oregon team led by evolutionary biologist Matt Barber, with doctoral student Titas Sil, used ancestral sequence reconstruction to synthesize antimicrobial peptides derived from lactoferrin as it existed in early placental mammals roughly 160 million years ago. The work was published in PLOS Biology on August 25, 2026, and publicized on September 28.
Several of the resurrected peptides were more potent against drug-resistant bacteria, including Pseudomonas aeruginosa and Staphylococcus aureus, than some modern human versions. A single amino acid change produced a substantial gain in antimicrobial activity, and progressively more recent ancestral versions showed progressively better performance. The oldest peptides could disrupt bacterial membranes, although bacteria eventually repaired the damage.
Why it matters: evolutionary history offers a new source of peptide leads for antibiotic-resistant infections, and the single-residue effect is a clean structure-activity story. Suggested PeptideWiki angle: a short explainer on lactoferrin-derived antimicrobial peptides and how ancestral reconstruction can guide peptide design.