These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: Analogues of cyclolinopeptide A containing alpha-hydroxymethyl amino acid residues.
    Author: Zubrzak P, Banaś A, Kaczmarek K, Leplawy MT, Sochacki M, Kowalski ML, Szkudlińska B, Zabrocki J, Di Lello P, Isernia C, Saviano M, Pedone C, Benedetti E.
    Journal: Biopolymers; 2005; 80(2-3):347-56. PubMed ID: 15614802.
    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.
    [Abstract] [Full Text] [Related] [New Search]