Weaving peptide nanonets to fight bacterial infections

Researchers at the National University of Singapore (NUS) have engineered self‑assembling peptides that trap fast‑moving Gram-negative bacteria, preventing their escape and helping to control infection.

Many harmful bacteria can move to evade high concentrations of antibiotics. This allows them to spread through the body and makes them harder to treat, contributing to the growing problem of drug-resistant infections. To tackle this, the research team led by Associate Professor Rachel EE Pui Lai from the NUS Department of Pharmacy and Pharmaceutical Sciences developed short peptides that can self-assemble into extremely fine fibres. These nanofibres weave together and form nanonets only in the presence of bacteria, trapping and killing them while leaving healthy cells untouched. By immobilising the bacteria, the nanonets prevent them from spreading and make them more vulnerable to existing antibiotics. The technology could inspire next‑generation biomaterials for wound dressings, coatings for medical devices or spray‑on treatments for bacterial infections.

Drawing inspiration from spiders that first weave expansive webs to catch prey and then wrap them tightly to prevent escape, the team focused on designing peptides that can form both extensive and tight nets depending on their amino acid sequence. In this study, they discovered that subtle changes in the peptide’s amino acids can control the way nanonets form. The peptide W-W₁₃ was engineered to form tightly interwoven nanofibres on bacteria surfaces, effectively trapping them in place and killing them. Another version, E-E₁₃^ASYM, was designed to self-interweave, forming wide-spanning nanonets with minimal bacterial interaction and no antibacterial activity. The team showed through laboratory tests that the tight nanonets could significantly inhibit bacterial movement, highlighting their potential in preventing the spread of infection.

The findings were published in the scientific journal Small on 7 July 2025.

Mr CHEN Wei Meng, a PhD candidate from the research team said, “Our findings show that with the right design, we can program these peptides to build nanonets tailored for specific antibacterial functions.”

“By simply teaching a peptide how to fold, we have given it the ability to immobilise bacteria before they can escape. Our next step is to translate this into a practical, low-cost solution to combat infections in real-world settings,” added Assoc Prof Ee.