Hybrid polymers bearing oligo-l-lysine(carboxybenzyl)s: synthesis and investigations of secondary structure.

Hybrid polymers of peptides resembling (partially) folded protein structures are promising materials in biomedicine, especially in view of folding-interactions between different segments. In this study polymers bearing repetitive peptidic folding elements, composed of N-terminus functionalized bis-ω-ene-functional oligo-l-lysine(carboxybenzyl(Z))s (Lys ) with repeating units () of 3, 6, 12, 24 and 30 were successfully synthesized to study their secondary structure introduced by conformational interactions between their chains. The pre-polymers of ADMET, narrowly dispersed Lys s, were obtained by ring opening polymerization (ROP) of -carboxyanhydride (NCA) initiated with 11-amino-undecene, following N-terminus functionalization with 10-undecenoyl chloride.

Secondary structure of end group functionalized oligomeric-l-lysines: investigations of solvent and structure dependent helicity.

Fibrillation of supramolecular building blocks represents an important model system for complex proteins and peptides, such as amyloidogenic proteins, displaying aggregation and subsequent collapse of their biological functions. In this work, we synthesized narrow-dispersed, end group-telechelic, oligomeric-(l-lysine(carboxybenzyl (Z)/trifluoroacetyl (TFA))) s ( = 3-33) as a model system for studying assembly and secondary structure formation, prepared ring opening polymerization (ROP) of -carboxyanhydrides (NCA). Our primary goal was to understand the influence of amino acid chain length and end group-modification on the secondary structure and fibrillation of the oligo-Z/TFA-protected lysines.