Overview

• The Rice University study, published September 10 in Nature Chemical Biology, introduces a live-cell probe that reports localized chemical changes tied to misfolding.
• Using genetic code expansion, researchers insert AnapTh at chosen residues without disrupting protein folding or function.
• Measurements of fluorescence intensity and spectral shifts show aggregation begins at discrete subdomain hot spots rather than uniformly across a protein.
• The approach provides site-specific, real-time readouts that existing bulk or late-stage techniques typically miss.
• The team, led by Han Xiao with co-authors including Mengxi Zhang and Shudan Yang, says the platform could enable earlier biomarker identification and real-time screening of aggregation inhibitors.