Analogues of cyclolinopeptide A containing alpha-hydroxymethyl amino acid residues |
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Authors: | Zubrzak Paweł Banaś Agnieszka Kaczmarek Krzysztof Leplawy Mirosław T Sochacki Marek Kowalski Marek L Szkudlińska Barbara Zabrocki Janusz Di Lello Paola Isernia Carla Saviano Michele Pedone Carlo Benedetti Ettore |
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Affiliation: | Institute of Organic Chemistry, Technical University of ?ód?, Zeromskiego 116, 90-924 ?ód?,Poland. |
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Abstract: | Linear and cyclic cyclolinopeptide A (CLA) analogues containing alpha-hydroxymethylleucine (HmL) in positions 1, 4, and 1&4, and alpha-hydroxymethylvaline (HmV) in position 5, were synthesized by the solid-phase peptide strategy and cyclized with the 1-Ethyl-3-(3-dimethylaminopropyl)-carbodiimide/1-hydroxy-7-azabenzotriazole (EDC/HOAt) reagent. The peptides were examined for their immunosuppressive activity in the lymphocyte proliferation assays (LPA). Only HmL-containing peptides demonstrated at about 25% lower immunosuppressive activity, but they are four times more soluble in water solutions than the native CLA. It seems from the LPA results that peptide [(HmL4)CLA] is the most promising for further studies. This peptide was characterized in solution, at room temperature in CDCl3, and the conformation compared with that observed for CLA in the solid state. |
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