Formation of left-handed helices in hybrid peptide oligomers with cis β-sugar amino acid and L-Ala as building blocks
Formation of left-handed helices in hybrid peptide oligomers with cis β-sugar amino acid and L-Ala as building blocks
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DOI：
10.1039/b612058j
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发表时间：
2007-01-01
影响因子：
4.9
通讯作者：
Jagannadh, Bulusu
中科院分区：
文献类型：
--
作者：
Jagadeesh, Bharatam;Prabhakar, Anabathula;Jagannadh, Bulusu
以L-Ala和顺式-b-呋喃糖氨基酸（FSAA）残基为构建块的杂化肽低聚物为基础，探索了基于残基的特定螺旋折叠控制；设计、合成了两个系列的杂化低聚物，并通过NMR、CD、FT-IR和MD模拟研究对其进行了广泛的表征；结果表明，Boc-(a/b)和Boc-(b/a)系列短聚物中存在左旋11-和14/15-螺旋构象。
Residue based control of specific helical folding is explored in hybrid peptide oligomers consisting of alternating L-Ala and cis-b-furanoid sugar amino acid (FSAA) residues as building blocks; two series of these hybrid oligomers are designed, synthesized and extensively characterized by using NMR, CD, FT-IR and MD simulation studies; results show the coexistence of left-handed 11- and 14/15-helical conformations in these short oligomers of Boc-(a/b) and Boc-(b/a) series.