Introduction to the Transdisciplinary International Conference on Aromatic Amino Acids and Related Substances: Chemistry, Biology, Medicine, and Application

Abstract

On the occasion of the ‘‘Transdisciplinary International Conference on Aromatic Amino Acids and Related Substances,’’ the organizing committee honors and thanks the expert participants from many areas of aromatic amino acid (AAA) 3 research. In this transdisciplinary meeting, ‘‘aromatic paradigms’’ were pursued in structural, molecular, information, and systems biology followed by papers on metabolism, pathology, and therapy in humans. Whereas basic biosciences invariably aim at coherent accounts of life as a highly complex yet united system, problemoriented approaches like medicine and nutrition study other aspects of the same reality. This conference holds an exceptional raison de e’tre, because all paradigms cut across the unique axis of ‘‘aromaticity,’’ eventually leading to a theoretical and experimental coherence. In 1991 K. Takai and 56 other scientists studying amino acids launched the first ‘‘Transdisciplinary International Conference on Amino Acid Research,’’ and held the initial congress in Kyoto, Japan (1) under the sponsorship of Ajinomoto Co., Inc. In the past 5 y, subsequent conferences have been held for glutamine (2), arginine (3), and branched chain amino acids (BCAA) (4). At the end of the last millennium, research on aromatic amino acids stepped into a newer stage. The cation-p interaction between the p-face of aromatic amino acids and cations was shown to constitute the fourth major, noncovalent chemical force in nature, along with those by hydrophobic effect/hydrogen bonding/ion pairing. Recent structural biology based on X-ray analyses of membrane/cytosolic protein crystals, solution NMR studies, thermodynamics of ligand-binding/permeation processes, mutation analyses, and computer-based methods for 3D structures from the primary protein structure verified that the cation-p interactions of electrostatic nature play crucial roles to support the macromolecular structure/recognition in life processes.