http://www.cnr.it/ontology/cnr/individuo/prodotto/ID13507
Analogues of cyclolinopeptide A containing a-hydroxymethyl amino acid residues. (Articolo in rivista)
- Type
- Label
- Analogues of cyclolinopeptide A containing a-hydroxymethyl amino acid residues. (Articolo in rivista) (literal)
- Anno
- 2005-01-01T00:00:00+01:00 (literal)
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Zubrzak, Pawel; Banas, Agnieszka; Kaczmarek, Krzysztof; Leplawy, Miroslaw T.; Sochacki, Marek; Kowalski, Marek L.; Szkudlinska, Barbara; Zabrocki, Janusz; Di Lello, Paola; Isernia, Carla; Saviano, Michele; Pedone, Carlo; Benedetti, Ettore. (2005)
Analogues of cyclolinopeptide A containing a-hydroxymethyl amino acid residues.
in Biopolymers (Print)
(literal)
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- Zubrzak, Pawel; Banas, Agnieszka; Kaczmarek, Krzysztof; Leplawy, Miroslaw T.; Sochacki, Marek; Kowalski, Marek L.; Szkudlinska, Barbara; Zabrocki, Janusz; Di Lello, Paola; Isernia, Carla; Saviano, Michele; Pedone, Carlo; Benedetti, Ettore. (literal)
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- Titolo
- Analogues of cyclolinopeptide A containing a-hydroxymethyl amino acid residues. (literal)
- Abstract
- Linear and cyclic cyclolinopeptide A (CLA) analogs contg. a-hydroxymethyl-leucine (HmL) in positions 1, 4, and 1 & 4, and a-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 examd. for their immunosuppressive activity in the lymphocyte proliferation assays (LPA). Only HmL-contg. peptides demonstrated at about 25% lower immunosuppressive activity, but they are four times more sol. in water solns. 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 soln., at room temp. in CDCl3, and the conformation compared with that obsd. for CLA in the solid state. (literal)
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