Hydrophobic Scale: a Second Parameter to Elucidating Various Specific Ligand–Protein Interactions

• Published in: Chemical & Pharmaceutical Bulletin Vol. 52; no. 3; pp. 377 - 379
• Main Authors: Numao, Naganori, Fujii, Hisashi, Fukazawa, Yoshiyuki, Hanagata, Nobutaka, Tanaka, Kazuyoshi
• Format: Journal Article
• Language: English; Japanese
• Published: Japan The Pharmaceutical Society of Japan 2004; Pharmaceutical Society of Japan
• Subjects: Amino Acid Sequence; Animals; Bone Morphogenetic Proteins - chemistry; Drosophila - chemistry; Escherichia coli - chemistry; Fibroblast Growth Factors - chemistry; Fourier Analysis; Humans; Ligands; Mice; Models, Molecular; Nucleotides - chemistry; Oryza - chemistry; Proteins - chemistry; Saccharomyces cerevisiae - chemistry; Sequence Analysis; Tumor Suppressor Protein p53 - chemistry
• ISSN: 0009-2363; 1347-5223
• DOI: 10.1248/cpb.52.377

In the sequence Fourier analysis (SFA) of specific interactions such as those between fibroblast growth factors (FGFs)/FGF receptors (FGFRs), bone morphogenetic proteins (BMPs)/BMP receptors (BMPRs), or tumor repressor protein p53/mouse double minute 2 homolog (MDM2), the characteristic frequency peak(s) could be observed with the hydrophobic scale for 20 amino acids as well as 4 nucleotides as the physicochemical parameter, but not successfully with the absolute electronegativity scale. This result implies that these two independent scales should be appropriately selected in various specific ligand–protein interactions, though the critical difference has to be determined.