(Cholestanyloxycarbonyl)benzyl esters as peptide substituents: Conformational properties of fully protected oligo-L-lysines with C-terminal (cholestanyloxycarbonyl)benzyl and benzyl ester moieties
✍ Scribed by Claudio Toniolo; Gian Maria Bonora; Vittorio Moretto; Conrad H. Schneider; Hanspeter Rolli; Marina Jung; Jan Izdebski
- Book ID
- 102256085
- Publisher
- John Wiley and Sons
- Year
- 1986
- Tongue
- German
- Weight
- 499 KB
- Volume
- 69
- Category
- Article
- ISSN
- 0018-019X
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✦ Synopsis
This study involves L-lysine oligo peptides, protected at the N-terminus by the Nps and at the &-amino functions by Boc groups. Two series were prepared from dimer to octamer, one containing the p-[(cholestan-3/3yloxy)carbonyl]benzyl, the other one the benzyl ester group at the C-terminus. Conformational analyses were performed by IR absorption. The occurrence of the intermolecular [i-structure in the solid state and in CHzC1, solution was demonstrated for the highest oligomers. The relative stabilities of the self-associated species were determined by adding a variety of polar solvents to the CHzC12 solutions. The cholestanyl-containing peptides have a lower propensity to self-aggregate than the bcnzyl-ester analogues. Self-aggregation and decreasing solubility run in parallel. It was also directly shown that soluble urea derivatives may disrupt intermolecular H-bonds in CH2CIz, a point of practical interest, particularly in solid-phase peptide synthesis.