Conformational studies on peptides having dipropylglycine (Dpg) or 1-aminocycloheptanecarboxylic acid (Ac7c) within the sequence of L-leucine (Leu) residues
Conformational studies on peptides having dipropylglycine (Dpg) or 1-aminocycloheptanecarboxylic acid (Ac7c) within the sequence of L-leucine (Leu) residues
复制标题
L-亮氨酸 (Leu) 残基序列中含有二丙基甘氨酸 (Dpg) 或 1-氨基环庚烷甲酸 (Ac7c) 的肽的构象研究
DOI：
10.1002/bip.22810
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发表时间：
2016
期刊：
影响因子：
--
通讯作者：
M. Tanaka
中科院分区：
文献类型：
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作者：
M. Oba;H. Nonaka;M. Doi;M. Tanaka
对含有1-亮氨酸(Leu)残基的二丙基甘氨酸(DPG)或1-氨基环庚烷羧酸(Ac7c)的多肽在溶液和结晶状态下进行了构象分析。DPG和Ac7c具有相似的结构，分别含有无环和环状侧链。红外光谱、核磁共振氢谱和圆二色谱测量表明，含有DPG-和Ac7c的L-Leu多肽在溶液中的优先构象相似，都具有右旋(P)310-螺旋。在晶态下，含DPG的八肽采用右旋(P)α-螺旋结构。DPG和Ac7c同源多肽分别以平面结构和螺旋结构为首选构象，而DPG-和Ac7c-L-Leu多肽在溶液中具有相似的结构。《威利期刊公司生物聚合物》(Pept Sci)106：210-218,2016。
A conformational analysis of peptides having dipropylglycine (Dpg) or 1‐aminocycloheptanecarboxylic acid (Ac7c) withinl‐leucine (Leu) residues was conducted in solution and in a crystal state. Dpg and Ac7c had similar structures with acyclic and cyclic side chains, respectively. FTIR,1H NMR, and CD spectra measurements revealed that the preferred conformations of Dpg‐ and Ac7c‐containingl‐Leu peptides in solution were similar; both had a right‐handed (P) 310‐helix. The Dpg‐containing octapeptide adopted a right‐handed (P) α‐helix in the crystal state. Dpg and Ac7c homopeptides had planar and helical structures as their preferred conformations, respectively; however, Dpg‐ and Ac7c‐containingl‐Leu peptides adopted similar structures in solution. © 2016 Wiley Periodicals, Inc. Biopolymers (Pept Sci) 106: 210–218, 2016.