The Ability of an α-Aminoisobutyric Acid Residue to Promote Helical Folding in Oligopeptides
The Ability of an α-Aminoisobutyric Acid Residue to Promote Helical Folding in Oligopeptides
复制标题
α-氨基异丁酸残基促进寡肽螺旋折叠的能力
DOI：
10.1246/bcsj.58.1731
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发表时间：
1985
影响因子：
4
通讯作者：
M. Doi
中科院分区：
文献类型：
--
作者：
M. Narita;K. Ishikawa;Hiroki Sugasawa;M. Doi
为了研究Aib残基促进寡肽中螺旋折叠的能力，通过逐步延伸和片段缩合方法制备含有Aib残基的寡（Leu）。制备的肽如下：Boc-Aib-Leun-OBzl（n=3-6和9）、Boc-Leun-Aib-OBzl（n=3-6和9）、Boc-Leu 3-Aib-Leu 3-OBzl、Boc-Leu 4-Aib-Leu 4-OBzl、Boc-Leu 8-Aib-Leu 4-OBzl、Boc-Leu 4-Aib-Leu 8-OBzl和Boc-Leu 8-Aib-Leu 8-OBzl。Boc-Aib-Leun-OBzl（n=3-6）在二氯甲烷中的红外吸收构象分析表明，由一个、两个、三个等i→i-4或i→i-3氢键模式形成的初始螺旋结构（α-或310-螺旋）的存在。除Boc-Aib-Leu 9-OBzl和Boc-Leun-Aib-OBzl（n=6和9）外，所有肽也显示出螺旋结构（α-或310-螺旋），表明Aib残基促进肽中螺旋折叠的巨大能力。这与同源寡聚（Leu）对应物具有β折叠结构的事实形成显著对比。...
In order to investigate the ability of an Aib residue to promote helical folding in oligopeptides, oligo(Leu)s containing an Aib residue were prepared by stepwise elongation and fragment condensation methods. The peptides prepared were the following: Boc–Aib–Leun–OBzl (n=3–6 and 9), Boc–Leun–Aib–OBzl (n=3–6 and 9), Boc–Leu3–Aib–Leu3–OBzl, Boc–Leu4–Aib–Leu4–OBzl, Boc–Leu8–Aib–Leu4–OBzl, Boc–Leu4–Aib–Leu8–OBzl, and Boc–Leu8–Aib–Leu8–OBzl. The IR absorption conformational analyses of Boc–Aib–Leun–OBzl (n=3–6) in dichloromethane have shown the occurrence of incipient helical structures (α- or 310-helixes) formed by one, two, three, and so forth i→i–4 or i→i–3 hydrogen-bonding patterns. All the peptides except Boc–Aib–Leu9–OBzl and Boc–Leun–Aib–OBzl (n=6 and 9) have also shown helical structures (α- or 310-helixes), indicating the great ability of an Aib residue to promote helical folding in peptides. This is in remarkable contrast with the fact that homologous oligo(Leu) counterparts have β-sheet structures. ...