Biological Consequences of the Incorporation of Amphiphilic Amino Acids into Opioid Peptide Sequences |
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| Authors: | Aleksandra Olma, Aleksandra Misicka, Dirk Tourwé Andrzej W. Lipkowski |
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| Affiliation: | (1) Institute of Organic Chemistry, Technical University, PL-90-924 Lodz, Poland;(2) Medical Research Centre, Polish Academy of Sciences, Pawinskiego 5, PL-02-106 Warsaw, Poland;(3) Industrial Chemistry Research Institute, Rydygiera 8, PL-01-793 Warsaw, Poland;(4) Department of Chemistry, Warsaw University, Pasteura 1, PL-02-093 Warsaw, Poland;(5) Organic Chemistry Laboratory, Vrije Universiteit Brussel, Brussel, Belgium |
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| Abstract: | Hydrophobic and aromatic interactions are most critical for membrane peptide receptor-ligand complex stability. We have hypothesized that proper location of hydrophilic counterparts to lipophilic and/or aromatic residues may stabilize complexation with the receptor pocket. In this work, we are presenting the biological consequences of introduction of a hydroxymethyl group into the  -position of phenylalanine or tyrosine residues of enkephalin or deltorphin analogues. The consequences of such a modification are strongly dependent on the position of the primary amino acid in the peptide chain. |
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| Keywords: | amphiphilic amino acid deltorphin enkephalin opioid |
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