Chain-length dependence for secondary structure formation of homo-oligopeptides from epsilon-tert.-butyloxycarbonyl-L-lysine with a lipophilic C-terminal group.
A solid-state and solution analysis of the homo-oligopeptides from epsilon-tert.-butyloxycarbonyl-L-lysine with p-oxymethylbenzylcholestan-3 beta-yl succinate as C-terminal group, using infrared absorption and circular dichroism, is described. The occurrence of intermolecular beta-structure is seen in the solid state and in solvents of low polarity, e.g. methylene chloride, for peptides of intermediate size (from pentamer to decamer). Conversely, the eicosapeptide exhibits a high percentage of alpha-helical structure both in the solid state and in 2,2,2-trifluoroethanol. The influence of the C-terminal group on the conformational preferences of the epsilon-blocked homo-oligolysines in the solid state and in organic solvents appears negligible.
D002855:Chromatography, Thin Layer; D002942:Circular Dichroism; D007202:Indicators and Reagents; D008239:Lysine / Q000031:analogs & derivatives*; D009842:Oligopeptides; D011487:Protein Conformation; D013055:Spectrophotometry, Infrared; D013329:Structure-Activity Relationship
D007202:Indicators and Reagents; D009842:Oligopeptides; C040741:epsilon-tert-butyloxycarbonyl-lysine; D008239:Lysine