A Solid-State Deuterium NMR and Sum-Frequency Generation Study of the Side-Chain Dynamics of Peptides Adsorbed onto Surfaces
A Solid-State Deuterium NMR and Sum-Frequency Generation Study of the Side-Chain Dynamics of Peptides Adsorbed onto Surfaces
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DOI：
10.1021/ja905382m
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发表时间：
2009-10-14
影响因子：
15
通讯作者：
Drobny, Gary P.
中科院分区：
文献类型：
--
作者：
Breen, Nicholas F.;Weidner, Tobias;Drobny, Gary P.
人工两亲肽LK α 14在界面处采用螺旋结构，其亮氨酸（L，疏水性）和赖氨酸（K，亲水性）侧链具有相反的取向。当肽被吸附到表面上时，不同的残基侧链必然具有与表面不同的接近度，这取决于它们在螺旋中的位置和表面本身的组成。氘化单个亮氨酸残基（异丙基-d（7））允许使用固态氘NMR光谱作为侧链动力学的位点特异性探针。结合和频生成作为探针的肽结合面，我们表明，特定的亮氨酸侧链在界面处的流动性是可量化的，在他们的表面接近。
The artificial amphiphilic peptide LK alpha 14 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.