Conformational studies of Ant–Pro motif-incorporated cyclic peptides: gramicidin S and avellanin†,New Journal of Chemistry

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Conformational studies of Ant–Pro motif-incorporated cyclic peptides: gramicidin S and avellanin†
New Journal of Chemistry ( IF 2.7 ) Pub Date : 2017-12-13 00:00:00 , DOI: 10.1039/c7nj03701e
Amol S. Kotmale _{1,

2,

3,

4,

5} , Ekta Sangtani _{2,

3,

4,

6} , Rajesh G. Gonnade _{2,

3,

4,

6} , Dhiman Sarkar _{4,

7,

8,

9,

10} , Sachin Burade _{4,

11,

12,

13} , Pattuparambil R. Rajamohanan _{2,

3,

4,

5} , Gangadhar J. Sanjayan _{1,

2,

3,

4}

Affiliation

This paper reports conformational changes observed in cyclic bioactive peptides such as gramicidin S and avellanin upon incorporation of a pseudo-β (C9) Ant–^DPro turn motif in their structural frameworks. Solution-state studies suggested that a synthetic gramicidin S analog exhibits a β-sheet conformation with C9 and C17 intramolecular hydrogen bonding patterns, while its truncated analog disturbs the β-sheet conformation. Structural details were obtained using a combination of CD studies, X-ray crystal structure studies and nOe-based MD simulation studies.

中文翻译：

Ant-Pro基序并入的环肽的构象研究：短杆菌肽S和avellanin †

本文报道了在其结构框架中掺入伪-β（C9）Ant– ^D Pro转位基序后，在诸如短杆菌肽S和avellanin等环状生物活性肽中观察到的构象变化。溶液状态研究表明，合成的短杆菌肽S类似物表现出具有C9和C17分子内氢键模式的β-折叠构象，而其截短的类似物干扰了β-折叠构象。通过结合CD研究，X射线晶体结构研究和基于nOe的MD模拟研究获得结构细节。

更新日期：2017-12-13

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