First Observation of Left-Handed Helical Conformation in a Dehydro Peptide Containing Two l-Val Residues. Crystal and Solution Structure of Boc-l-Val-ΔPhe-ΔPhe-ΔPhe-l-Val-OMe†,⊥
First Observation of Left-Handed Helical Conformation in a Dehydro Peptide Containing Two l-Val Residues. Crystal and Solution Structure of Boc-l-Val-ΔPhe-ΔPhe-ΔPhe-l-Val-OMe†,⊥
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首次观察含有两个 l-Val 残基的脱氢肽中 Boc-l-Val-ΔPhe-ΔPhe-ΔPhe-l-Val-OMe†,⊥ 的溶液结构。
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发表时间：
1997
期刊：
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通讯作者：
Virander S. Chauhan
中科院分区：
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作者：
R. Jain;K. Rajashankar;S. Ramakumar;Virander S. Chauhan
用x射线衍射、核磁共振和圆二色法测定了含有三个连续Delta Phe残基的Boc-L-Val-Delta Phe-Delta Phe-Delta Phe- l- val - ome的溶液结构和固体结构。在甲醇水溶液中生长的晶体为正交晶系，空间群为P2(1)2(1)2(1)，空间群为a = 11.624(2), b = 17.248(2), c = 21.532埃，V = 4216(1)埃(3),Z = 4。在固体状态下，尽管存在两个L-Val残基，肽仍表现出左旋3(10)-螺旋构象。在不同溶剂中的NMR和CD研究也支持晶体结构数据，表明溶液中也保持了固态结构。这是首次报道含有三个连续的Delta Phe残基的脱氢肽，并表现出左旋3(10)-螺旋构象，这表明在肽中连续出现Delta Phe残基所产生的显着构象后果。
The solution and solid structure of Boc-L-Val-Delta Phe-Delta Phe-Delta Phe-L-Val-OMe, containing three consecutive Delta Phe residues, have been determined by X-ray diffraction, nuclear magnetic resonance, and circular dichroism methods. The crystals grown from aqueous methanol are orthorhombic, space group P2(1)2(1)2(1), a = 11.624(2), b = 17.248(2), c = 21.532 Angstrom, V = 4216 (1) Angstrom(3), Z = 4. In the solid state, the peptide exhibits a left-handed 3(10)-helical conformation, in spite of the presence of two L-Val residues. NMR and CD studies in different solvents also support the crystal structure data, suggesting that the solid state structure is maintained in solution as well. This is the first report of a dehydropeptide containing three consecutive Delta Phe residues and exhibiting left-handed 3(10)-helical conformation, which demonstrates the remarkable conformational consequences produced by consecutive occurrence of Delta Phe residues in a peptide.