Preliminary study on application of impregnated synthetic peptide TLC stationary phases for the pre-screening of 5-HT1A ligands

• Published in: Biomedical chromatography 2003-07, Vol.17 (5), p.312-317
• Main Authors: Zajdel, PaweŁ, Bojarski, Andrzej J., Byrtus, Hanna, ChŁoń-Rzepa, Grażyna, Obniska, Jolanta, Chevallet, Pierre, Martinez, Jean, PawŁowski, Maciej
• Format: Article
• Language: English
• Subjects: 5-HT1A receptor affinity; Amino Acid Sequence; arylpiperazine derivatives; Aspartic Acid - chemistry; binding constants; biospecific binding; Buffers; Chromatography, Affinity - methods; Chromatography, Thin Layer - methods; Hydrophobic and Hydrophilic Interactions; Ligands; Membrane Proteins - chemistry; Membrane Proteins - isolation & purification; Molecular Structure; Peptides - chemical synthesis; Peptides - chemistry; Peptides - metabolism; Pilot Projects; Piperazines - chemistry; protein-based affinity chromatography; Receptors, Serotonin - chemistry; Receptors, Serotonin - metabolism; Structure-Activity Relationship
• ISSN: 0269-3879; 1099-0801
• DOI: 10.1002/bmc.224

Chromatographic parameters (ΔRf), defined as a difference in the migration of tested compound on the control and peptide impregnated silica gel TLC plates, were determined for 42 arylpiperazine derivatives. An amino acid sequence of the peptide used for impregnation was derived from the III transmembrane segment of the 5‐HT1A receptor in the close vicinity of aspartic acid (Asp 166) residue. It was found that the ΔRf values obtained in a model employing tetrapeptide P4LA (ADVL), as well as the calculated logP correlate with 5‐HT1A receptor affinity of the studied compounds. Copyright © 2003 John Wiley & Sons, Ltd.