Repozytorium

Effect of the ΔPhe residue configuration on a didehydropeptides conformation: a combined CD and NMR study.

Autorzy

Marek Lisowski

Łukasz Jaremko

Mariusz Jaremko

Adam Mazur

Rafał Latajka

Maciej Makowski

Rok wydania

2010

Czasopismo

Biopolymers

Numer woluminu

93

Strony

1055-1064

DOI

10.1002/bip.21522.

Kolekcja

Naukowa

Język

Angielski

Typ publikacji

Artykuł

Streszczenie

Conformations of two pairs of dehydropeptides with the opposite configuration of the ΔPhe residue, Boc-Gly-Δ(Z)Phe-Gly-Phe-OMe (Z-OMe), Boc-Gly-Δ(E)Phe-Gly-Phe-OMe (E-OMe), Boc-Gly-Δ(Z)Phe-Gly-Phe-p-NA (Z-p-NA), and Boc-Gly-Δ(E)Phe-Gly-Phe-p-NA (E-p-NA) were compared on the basis of CD and NMR studies in MeOH, trifluoroethanol (TFE), MeCN, chloroform, and dimethylsulfoxide (DMSO). The CD results were used as the additional input data for the NMR-based determination of the detailed solution conformations of the peptides. It was found that E-OMe is unordered and Z-OMe, Z-p-NA, and E-p-NA adopt the β-turn conformation. There are two overlapping β-turns in each of those peptides: type II and type III' in Z-OMe and Z-p-NA, and two type III in E-p-NA. The ordered structure-inducing properties of Δ(Z)Phe and Δ(E)Phe in the peptides studied depend on the C-terminal blocking group. In methyl esters, the Δ(Z)Phe residue is a strong inducer of ordered conformations whereas the Δ(E)Phe one has no such properties. In p-nitroanilides, both isomers of ΔPhe cause the peptides to adopt ordered structures to a similar extent.

Adres publiczny

http://dx.doi.org/10.1002/bip.21522.

Strona internetowa wydawcy

onlinelibrary.wiley.com

Podobne publikacje
2008

Combined effect of the ΔPhe or ΔAla residue and thep-nitroanilide group on a didehydropeptides conformation.

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2007