A solid-state deuterium NMR and sum-frequency generation study of the side-chain dynamics of peptides adsorbed onto surfaces

Citation

Breen, Nicholas F.; Weidner, Tobias; Li, Kun; Castner, David G.; & Drobny, Gary P. (2009). A solid-state deuterium NMR and sum-frequency generation study of the side-chain dynamics of peptides adsorbed onto surfaces. J Am Chem Soc, 131(40), 14148-14149.

Abstract

The artificial amphiphilic peptide LKalpha14 adopts a helical structure at interfaces, with opposite orientation of its leucine (L, hydrophobic) and lysine (K, hydrophilic) side chains. When peptides are adsorbed onto surfaces, different residue side chains necessarily have different proximities to the surface, depending on both their position in the helix and the composition of the surface itself. Deuterating the individual leucine residues (isopropyl-d(7)) permits the use of solid-state deuterium NMR spectroscopy as a site-specific probe of side-chain dynamics. In conjunction with sum-frequency generation as a probe of the peptide-binding face, we demonstrate that the mobility of specific leucine side chains at the interface is quantifiable in terms of their surface proximity.

Keyword(s)

Adsorption
Amino Acid Sequence
Deuterium
Hydrophobic and Hydrophilic Interactions
Leucine
Lysine
Models, Molecular
Nuclear Magnetic Resonance, Biomolecular
Peptides

Reference Type

Journal Article

Secondary Title

J Am Chem Soc

Author(s)

Breen, Nicholas F.
Weidner, Tobias
Li, Kun
Castner, David G.
Drobny, Gary P.

Year Published

2009

Date Published

1255478400

Volume Number

131

Issue Number

40

Pages

14148-14149

ISSN/ISBN

1520-5126

DOI

10.1021/ja905382m