Folding of a Linear Array of 伪-Amino Acids within a Helical Aromatic Oligoamide Frame

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• 作者：Mayumi Kudo ; Victor Maurizot ; Brice Kauffmann ; Aya Tanatani ; Ivan Huc
• 刊名：The Journal of the American Chemical Society
• 出版年：2013
• 出版时间：July 3, 2013
• 年：2013
• 卷：135
• 期：26
• 页码：9628-9631
• 全文大小：259K
• 年卷期：v.135,no.26(July 3, 2013)
• ISSN：1520-5126

文摘

Control of the spatial organization of proteinogenic side chains is critical for the development of protein mimics with selective recognition properties toward target protein surfaces. We present a novel methodology for producing a linear array of proteinogenic residues based on the incorporation of 伪-amino acids into sequences of rigid, helically folded oligoamides of 8-amino-2-quinolinecarboxylic acid (Q). When l-leucine (L) was alternated with dimer Q₂, the resulting sequence adopted a right-handed helical conformation, as deduced in solution from the CD spectra of l-(LQ₂)_n (n = 2, 4) and in the solid state from X-ray crystallographic analysis of (卤)-(LQ₂)₄. Each LQ₂ segment spanned just one helix turn (pitch of 3.5 脜), and consequently, the four leucine side chains of (LQ₂)₄ formed a linear array. In solution, NMR analysis showed that both l-(LQ₂)₂ and l-(LQ₂)₄ exist as a mixture of two slowly equilibrating folded conformers, the proportion of which strongly varies with the solvent.