Institute of Organic Chemistry, Technical University of d, Zeromskiego 116 Str., 90-924 d, Poland
Molecular and Macromolecular Research Center, Polish Academy of Sciences, Sienkiewicza 112, 90-363 d, Poland
Medical University of d, Departement of Immunology, Mazowiecka 11, 92-215 d, Poland
Dipartimento di Scienze Ambientali, Seconda Universit di Napoli, Caserta 81100, Italy
Istituto di Biostrutture e Bioimmagini, CNR and Dipartimento di Chimica Biologica, Universit degli Studi di Napoli Federico II, Napoli 80134, Italy
References: Not available.
Analogues of cyclolinopeptide A containing alpha-hydroxymethyl amino acid residues
Linear and cyclic cyclolinopeptide A (CLA) analogues containing -hydroxymethyl-leucine (HmL) in positions 1, 4, and 1& 4, and -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 CDCl 3, and the conformation compared with that observed for CLA in the solid state. 2004 Wiley Periodicals, Inc
Analogues of cyclolinopeptide A containing alpha-hydroxymethyl amino acid residues
Malvindi MA, Greco A, Conversano F, Figuerola A, Corti M, Bonora M, Lascialfari A, Doumari HA, Moscardini M, Cingolani R, Gigli G, Casciaro S, Pellegrino T, Ragusa A * MR Contrast Agents(365 views) Small Animal Imaging, 2011 Jul 8; 21(13): 2548-2555. Impact Factor:1.784 ViewExport to BibTeXExport to EndNote