Solid-State Conformation of a Hybrid Tripeptide between .BETA.-Amino Acid; 8-Aminocyclooct-4-enecarboxylic Acid and 2-Aminoisobutyric Acid.
Masakazu Tanaka, Makoto Oba, Takaharu Ichiki, Hiroshi Suemune
Abstract
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Masakazu Tanaka, Makoto Oba, Takaharu Ichiki, Hiroshi Suemune
Abstract
Open-access reader
An eight-membered cyclic beta-amino acid, 8-aminocyclooct-4-enecarboxylic acid, was designed as a conformationally restricted non-proteinogenic amino acid. A hybrid tripeptide containing this eight-membered cyclic beta-amino acid and 2-aminoisobutyric acids was synthesized by conventional solution methods. The conformation of the tripeptide was studied using X-ray analysis and was shown to form an eleven-membered hydrogen-bonded turn (3(11)-helical structure) in the solid state.
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An eight-membered cyclic beta-amino acid, 8-aminocyclooct-4-enecarboxylic acid, was designed as a conformationally restricted non-proteinogenic amino acid. A hybrid tripeptide containing this eight-membered cyclic beta-amino acid and 2-aminoisobutyric acids was synthesized by conventional solution methods. The conformation of the tripeptide was studied using X-ray analysis and was shown to form an eleven-membered hydrogen-bonded turn (3(11)-helical structure) in the solid state.
Key concepts: Tripeptide, Chemistry, Aminoisobutyric acid, Amino acid, Stereochemistry, Oligopeptide, Solid-state, Peptide