Predictable Conformational Diversity in Foldamers of Sugar Amino Acids

K. Menyhárd, Dóra and Hudaky, Ilona and Jákli, Imre and Juhász, György and Perczel, András (2017) Predictable Conformational Diversity in Foldamers of Sugar Amino Acids. JOURNAL OF CHEMICAL INFORMATION AND MODELING, 57 (4). pp. 757-768. ISSN 1549-9596


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Systematic conformational search was carried out for monomers and homohexamers of furanoid β-amino acids: cis-(S,R) and trans-(S,S) stereoisomers of aminocyclopentane carboxylic acid (ACPC), two different aminofuranuronic-acids (AFU(alpha) and AFUβ), their isopropylidene derivatives (AFU(ip)) as well as the key intermediate β-aminotetrahydrofurancarboxylic acid (ATFC). Stereochemistry of the building blocks was chosen to match with that of natural sugar amino acid (xylose and ribose) precursors (XylAFU and RibAFU). Results show that hexamers of cis furanoid beta-amino acids show great variability: while hydrophobic cyclopentane (cis(ACPC)6), and hydrophilic (XylAFU(alpha)/(beta))6 foldamers favor two different zigzagged conformation as hexamers, the backbone fold turns into a helix in case of (cisATFC)6 (10-helix) and (XylAFU(ip))6 (14-helix). Trans stereochemistry resulted in hexamers exclusively of right-handed helix conformation, (H12P)6, regardless of their polarity. We found that the preferred oligomeric structure of XylAFU(alpha)/(beta) is conformationally compatible with beta-pleated sheets, while that of the trans/(S,S) units match with alpha-helices of proteins.

Item Type: Article
Subjects: Q Science / természettudomány > QD Chemistry / kémia > QD04 Organic chemistry / szerves kémia
Depositing User: Dóra K. Menyhárd
Date Deposited: 14 Feb 2018 13:47
Last Modified: 01 Jan 2019 00:15

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