Molecular Design of β‐Sheet Peptide for Multi‐Modal Analysis of Disease

Intermolecular forces fundamentally constrain peptide conformation. However, the exact role of each intermolecular force in constraining peptide conformation remains poorly understood. In this work, we uncover that aromatic‐aromatic interactions predominantly drive peptides into β‐sheets, and hydrophobic effect fundamentally determines the assembly speed of peptides. By using intermolecular forces to artificially control the rapid assembly of β‐sheets, we develop a multi‐modal analytical system which allows five readouts and dual qualitative‐quantitative analysis, and satisfies both point‐of‐care testing (POCT) and laboratory‐based testing. For Mycoplasma Pneumoniae diagnosis, in comparison to conventional methods, this multi‐modal analytical system completely eradicates misdiagnosis (from 30% to 0%) and broadens linear range by three fold, both of which are critical for guiding therapy. This work not only illustrates exact roles of intermolecular forces in driving the formation of β‐sheets, but also provides a guideline to construct a multi‐modal analytical system for disease diagnosis that no other approaches have been able to achieve so far.

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