Conformational preferences of oligopeptides rich in alpha-aminoisobutyric acid. III. Design, synthesis and hydrogen bonding in 3(10)-helices.
Conformational preferences of oligopeptides rich in alpha-aminoisobutyric acid. III. Design, synthesis and hydrogen bonding in 3(10)-helices.
复制标题
富含α-氨基异丁酸的寡肽的构象偏好。
DOI：
10.1111/j.1399-3011.1994.tb01142.x
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发表时间：
1994
期刊：
影响因子：
--
通讯作者：
Kuki,A
中科院分区：
文献类型：
--
作者：
Bindra,VA;Kuki,A
用优化的{iBoc‐Aib‐Aib‐Aib‐DkNap‐Leu‐Qx‐Ala‐Aib‐Aib‐F1，/HOBt方法合成了两个空间受限多肽andiBoc‐Aib‐Aib‐Aib‐DkNap‐Leu‐Aib‐Ala‐Aib‐Aib‐Fl，(Dk4Qx6[7/9])α(Dk47/9)}，其中含有α-氨基异丁酸和AiB类氨基酸。使用这里定义和讨论的AIB类氨基酸(例如DkNap和Qx)，可以产生与更简单的富含AIB的多肽和同源多肽相同的压倒性310-螺旋骨架构象。人工合成的α，α-二烷基氨基酸(DkNap，Qx)是已知的AiB的脂环变体Ac5c和Ac6c的芳香族同系物。介绍了两种新的多肽有机增溶基团iBoc和2-甲氧基乙胺。Dk4s/p[7/9]和Dk4Qx6[7/9]多肽的1H核磁共振分析表明，这些多肽具有明确的310S/b螺旋氢键模式，证实了这些序列模式的设计目标，这些序列模式含有大于50%的AIB和AIB类组成。©孟克斯加德1994年。
Two sterically constrained peptides {iBoc‐Aib‐Aib‐Aib‐DkNap‐Leu‐Qx‐Ala‐Aib‐Aib‐F1, (Dk4Qx6[7/9]) andiBoc‐Aib‐Aib‐Aib‐DkNap‐Leu‐Aib‐Ala‐Aib‐Aib‐Fl, (Dk47/9)} containing α‐aminoisobutyric acid (Aib) and Aib‐class amino acids in conjunction with selected mono‐α‐alkyl amino acids were synthesized by an optimized TBTU/HOBt procedure. The use of Aib‐class amino acids (e.g.DkNap and Qx), defined and discussed here, gives rise to the same overwhelmingly 310‐helical backbone conformation as that provided by simpler Aib‐rich peptides and homopeptides. The synthetic α,α‐dialkylamino acids (DkNap, Qx) are aromatic homologues of the known alicyclic variants of Aib, the Ac5c and Ac6c amino acids. Two new organic solubilizing groups for peptides,iBoc and 2‐methoxyethylamine, are introduced. The1H nuclear magnetic resonance analyses of the Dk4s/p[7/9] and Dk4Qx6[7/9] peptides demonstrate the unambiguous 310s/b‐helical hydrogen bonding pattern of these peptides, confirming the design objective of these sequence patterns containing greater than 50% Aib and Aib‐class composition. © Munksgaard 1994.