Abstract
We have developed a group of branched (multichain) poly-peptides composed of a poly(L-lysine) backbone with short oligomeric poly(DL-alanine) side chains (the inside area) and one, two or more other amino acid residues (the outside determinant). These polypeptides were characterized by amino acid analysis, identification of terminal amino acids of the side chains, sedimentation analysis, and thin-layer and column gel chromatography. The conformation of the polypeptides was analyzed by circular dichroism spectroscopy of water-alcohol mixtures and of water solutions at various pH and ionic strengths. These data indicated a marked dependence of the conformation on the identity, charge and absolute configuration of the side chain terminal amino acids and on the number of these residues present. The immunomodulatory potential of one of these polypeptides was investigated. Dose dependence, immunization schedule and ability of this polypep-tide to compensate for the immunosuppressive effect of cyto-toxic drugs were evaluated.
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Hudecz, F. et al. (1985). Branched Polypeptides with a Poly(L-Lysine) Backbone: Synthesis, Conformation, and Immunomodulation. In: Gebelein, C.G., Carraher, C.E. (eds) Polymeric Materials in Medication. Polymer Science and Technology, vol 32. Springer, Boston, MA. https://doi.org/10.1007/978-1-4899-2245-8_22
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DOI: https://doi.org/10.1007/978-1-4899-2245-8_22
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