Department of Biochemistry and Biophysics, University of Pennsylvania, Philadelphia, Pennsylvania 19104, United States.
Org Lett. 2010 Nov 19;12(22):5142-5. doi: 10.1021/ol102092r. Epub 2010 Oct 14.
The first computationally designed self-assembling oligomer consisting of exclusively β-amino acids (βAAs) is presented. The packing of a β-3(14) helix into coiled-coils of varying stoichiometries as a function of amino acid sequence is examined. β-Peptides with hVal repeating every third residue in the sequence appeared to have a strong propensity to pack into hexameric bundles. The designed sequence was synthesized and characterized with CD spectroscopy, NMR, and analytical ultracentrifugation, suggesting that the peptide adopts a well-folded hexameric structure.
首次提出了仅由β-氨基酸（βAAs）组成的首个计算设计的自组装低聚物。研究了β-3（14）螺旋作为氨基酸序列的函数在不同化学计量比的螺旋-螺旋中的包装。在序列中每隔三个残基重复 hVal 的β-肽似乎具有强烈的倾向，以六聚体束的形式包装。设计的序列通过 CD 光谱，NMR 和分析超速离心进行了合成和表征，表明该肽采用了折叠良好的六聚体结构。
