Enantioselective Lanthanide Binding Modulates Collagen Self‐Assembly

ABSTRACT Collagen fibrillogenesis underlies the structural and mechanical properties of the extracellular matrix in connective and other tissues, yet its molecular mechanism remains poorly understood. Here, we show that a europium(III) dipicolinate complex (EuDPA) acts as a luminescent reporter of collagen aggregation. We combine Raman microscopy, circularly polarized luminescence (CPL), and molecular dynamics (MD) simulations to study this process. While Raman imaging directly visualizes the EuDPA‐enhanced fibrillar architecture, CPL reveals enantioselective EuDPA–collagen interactions that accompany the fibrillogenesis. MD simulations indicate the presence of stabilizing interactions between hydroxyproline residues and the dipicolinate ligand. The results pave the way to monitoring of protein aggregation in general, and are relevant to fibrotic pathologies and biomimetic materials design.