oa South African Journal of Chemistry - Conformational comparison of cyclic α3β tetrapeptide vs. α3β pentapeptide : research article
|Article Title||Conformational comparison of cyclic α3β tetrapeptide vs. α3β pentapeptide : research article|
|© Publisher:||South African Chemical Institute (SACI)|
|Journal||South African Journal of Chemistry|
|Affiliations||1 University of KwaZulu-Natal, 2 University of KwaZulu-Natal, 3 University of KwaZulu-Natal, 4 University of KwaZulu-Natal, 5 University of KwaZulu-Natal, 6 University of Pune, India, 7 University of Pune, India and 8 University of Barcelona, Spain|
|Publication Date||Jan 2014|
|Pages||80 - 84|
|Keyword(s)||CD spectroscopy, Conformational analysis, Cyclic peptide, NMR spectroscopy, Pentapeptide and Tetrapeptide|
The γ-turn inducing sugar α-amino acid plays an important role in the formation of well-defined secondary structures of cyclic tetra- and pentapeptide. Two tetra- and one novel pentapeptide were synthesized from a sugar α-amino acid and the conformations of the compounds were established by NMR spectroscopy (EASY-ROESY) and compared with CD spectroscopic data. Although the γ-turn conformation was dominant for both tetra- and pentapeptide according to NMR spectroscopic analysis in DMSO, the pentapeptide exhibited the presence of a second conformation. CD spectroscopic results in methanol showed that the tetrapeptides have a γ-turn conformation, while the pentapeptide has a random structure.
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