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 α-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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Olma, A., Misicka, A., Tourwé, D. et al. Biological Consequences of the Incorporation of Amphiphilic Amino Acids into Opioid Peptide Sequences. Letters in Peptide Science 5, 383–385 (1998). https://doi.org/10.1023/A:1008812213613
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DOI: https://doi.org/10.1023/A:1008812213613