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For investigations of adsorption of polymers onto surfaces, lysine oligomers of defined lengths were synthesized using standard methods of peptide chemistry. By repeated coupling of peptide derivatives of the same length, peptide chains up to 32 lysine residues were obtained. To suppress end effects the N-terminal a-amino group and the carboxyl group of each peptide were blocked with e-aminocaproyl-and N-methylamide functions respectively. Measurements of the optical rotation of blocked and charged deblocked oligo-L-lysines indicated that ordered structures are present in both forms.