[NMR paper] Studying the Conformation of a Silaffin-Derived Pentalysine Peptide Embedded in Bioinspired Silica using Solution and DNP MAS NMR.

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Studying the Conformation of a Silaffin-Derived Pentalysine Peptide Embedded in Bioinspired Silica using Solution and DNP MAS NMR.

Related Articles Studying the Conformation of a Silaffin-Derived Pentalysine Peptide Embedded in Bioinspired Silica using Solution and DNP MAS NMR.

J Am Chem Soc. 2015 Oct 9;

Authors: Geiger Y, Gottlieb HE, Akbey Ü, Oschkinat H, Goobes G

Abstract
Smart materials are created in nature at interfaces between biomolecules and solid materials. The ability to probe the structure of functional peptides that engineer biogenic materials at this heterogeneous setting can be facilitated tremendously by use of DNP-enhanced solid-state NMR spectroscopy. This sensitive NMR technique allows simple and quick measurements, often without the need for isotope enrichment. Here, it is used to characterize a pentalysine peptide, derived from a diatom's silaffin protein. The peptide accelerates the formation of bio-inspired silica and gets embedded inside the material as it is formed. 2D DNP MAS-NMR of the silica-bound peptide and solution NMR of the free peptide are used to derive its secondary structure in the two states and to pinpoint some subtle conformational changes that the peptide undergoes in order to adapt to the silica environment. In addition, interactions between abundant lysine residues and silica surface are identified and proximity of other sidechains to silica and to neighboring peptide molecules is discussed.


PMID: 26451953 [PubMed - as supplied by publisher]



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