Improved resolution in two-dimensional 1H NMR spectra of peptides by band-selective, homonuclear decoupling during both the evolution and acquisition periods: application to characterization of the binding of peptides by heparin.
Improved resolution in two-dimensional 1H NMR spectra of peptides by band-selective, homonuclear decoupling during both the evolution and acquisition periods: application to characterization of the binding of peptides by heparin.
复制标题
通过在进化和采集期间的带选择性、同核解偶联提高肽的二维 1H NMR 谱的分辨率：应用于肝素肽结合的表征。
DOI：
10.1002/mrc.1842
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发表时间：
2006
期刊：
影响因子：
--
通讯作者：
Rabenstein,DallasL
中科院分区：
文献类型：
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作者：
Wang,Jing;Borchardt,Dan;Rabenstein,DallasL
使用在间接检测的F1和直接检测的F2维度中实现带选择性、同源解耦的二维1H NMR实验来分配肽Ac-SRGKARVRAKVKDQTK-NH 2的高度重叠的1H NMR光谱，所述肽Ac-SRGKARVRAKVKDQTK-NH 2在溶液中游离并与肝素结合。使用具有半选择性成形脉冲的双脉冲场梯度自旋回波（DPFGSE）实现了演化期间的频带选择性均匀去耦;通过分时半选择性成形脉冲去耦实现了采集期间的频带选择性均匀去耦。报告并比较了肽及其肝素复合物的常规TOCSY、ROESY和NOESY光谱，以及在演化（F1）维度（BASHD-TOCSY、ROESY和NOESY光谱）中采用带选择性同源解耦测量的TOCSY、ROESY和NOESY光谱，以及在F1和F2维度（D-（或双）-BASHD-TOCSY、ROESY和NOESY光谱）中采用带选择性同源解耦测量的TOCSY、ROESY和NOESY光谱。通过D-BASHD-TOCSY、ROESY和NOESY光谱的高分辨率，实现了游离肽和肝素复合肽的1H-NMR光谱的完全归属。肝素复合肽的表征是令人感兴趣的，因为肽能够中和肝素的抗凝活性。版权所有© 2006约翰威利父子有限公司。
Two‐dimensional1H NMR experiments that achieve band‐selective, homonuclear decoupling in both the indirectly detected F1 and directly detected F2 dimensions were used to assign the highly overlapped1H NMR spectrum of the peptide Ac‐SRGKARVRAKVKDQTK‐NH2, both free in solution and bound to heparin. Band‐selective, homonuclear decoupling during the evolution period was achieved using a double pulsed field gradient spin‐echo (DPFGSE) with semi‐selective shaped pulses; band‐selective, homonuclear decoupling during the acquisition period was achieved by time‐shared semi‐selective shaped pulse decoupling. Regular TOCSY, ROESY and NOESY spectra and TOCSY, ROESY and NOESY spectra measured with band‐selective, homonuclear decoupling in the evolution (F1) dimension (BASHD‐TOCSY, ROESY and NOESY spectra) and with band‐selective, homonuclear decoupling in both the F1 and F2 dimensions (D‐(or Double)‐BASHD‐TOCSY, ROESY and NOESY spectra) are reported and compared for the peptide and its heparin complex. Complete assignment of the1H‐NMR spectra of the free and heparin‐complexed peptide was achieved with the high resolution of the D‐BASHD‐TOCSY, ROESY and NOESY spectra. Characterization of the heparin‐complexed peptide is of interest because of the ability of the peptide to neutralize the anticoagulant activity of heparin. Copyright © 2006 John Wiley & Sons, Ltd.