Structural Insights into Peptides Bound to the Surface of Silica Nanopores

Abstract

The structure and surface functionalization of biologically relevant silica-based hybrid materials was investigated by 2D solid-state NMR techniques combined with dynamic nuclear polarization (DNP). This approach was applied to a model system of mesoporous silica, which was modified through in-pore grafting of small peptides by solid-phase peptide synthesis (SPPS). To prove the covalent binding of the peptides on the surface, DNP-enhanced solid-state NMR was used for the detection of ¹⁵ N NMR signals in natural abundance. DNP-enhanced heterocorrelation experiments with frequency switched Lee-Goldburg homonuclear proton decoupling (¹ H-¹³ C and ¹ H-¹⁵ N CP MAS FSLG HETCOR) were performed to verify the primary structure and configuration of the synthesized peptides. ¹ H FSLG spectra and ¹ H-²⁹ Si FSLG HETCOR correlation spectra were recorded to investigate the orientation of the amino acid residues with respect to the silica surface. The combination of these NMR techniques provides detailed insights into the structure of amino acid functionalized hybrid compounds and allows for the understanding for each synthesis step during the in-pore SPPS.

Keywords: biomineralization; dynamic nuclear polarization; hybrid materials; mesoporous silica; solid-phase peptide synthesis.