Measurements of residual dipolar couplings in peptide inhibitors weakly aligned by transient binding to peptide amyloid fibrils

被引:11
作者
Chen, ZJ
Reif, B
机构
[1] Forschungsinst Mol Pharmakol, D-13125 Berlin, Germany
[2] Humboldt Univ, Charite Univ Med, D-10117 Berlin, Germany
[3] Tech Univ Munich, Inst Organ Chem & Biochem 2, D-85747 Garching, Germany
关键词
Alzheimer's disease; amyloid fibril; beta-sheet breaker peptide; inhibitors of fibril formation; protein aggregation; solution state NMR spectroscopy; transferred residual dipolar coupling; trRDC;
D O I
10.1023/B:JNMR.0000034353.98902.4f
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
In this communication, we suggest that transferred residual dipolar couplings (trRDCs) can be employed to restrain the structure of peptide inhibitors transiently binding to beta-amyloid fibrils. The effect is based on the spontaneous alignment of amyloid fibrils with the fibril axis parallel to the magnetic field. This alignment is transferred to the transiently binding peptide inhibitor and is reflected in the size of the trRDCs. We find that the peptide inhibitor adopts a beta-sheet conformation with the backbone N-H and C-H dipolar vectors aligned preferentially parallel and perpendicular, respectively, to the fibril axis.
引用
收藏
页码:525 / 530
页数:6
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