Amino Acids and Peptides. XXXIII. Synthesis of N-Terminal Epitope Peptides of Mammalian Metallothioneins (MTs)

• Published in: Chemical & pharmaceutical bulletin Vol. 40; no. 4; pp. 1029 - 1032
• Main Authors: TERAO, Tadao, NAKAYAMA, Shigeru, KIKUCHI, Yutaka, SAWADA, Jun-ichi, OKADA, Yoshio, IRIE, Masachika, IGUCHI, Shin, IKEBUCHI, Hideharu
• Format: Journal Article
• Language: English
• Published: Japan The Pharmaceutical Society of Japan 1992; 公益社団法人日本薬学会; Japan Science and Technology Agency
• Subjects: Amino Acid Sequence; Amino Acids - chemical synthesis; Animals; Epitopes; Metallothionein - chemical synthesis; Metallothionein - immunology; Molecular Sequence Data; Peptide Fragments - chemical synthesis; Peptide Fragments - immunology
• ISSN: 0009-2363; 1347-5223; 1347-5223
• DOI: 10.1248/cpb.40.1029

In order to determine the fine structure of the mammalian metallothionein (MT) epitope to a monoclonal anti-rat Zn-MT-II antibody (MT 189-14-7), N-terminal peptides of various lengths of mammalian metallothioneins (MTs) were synthesized by a conventional solution method using the newly developed beta-2-adamantylaspartate, and their immunological properties were examined. It was found that the N-terminal acetyl group was indispensable for the reaction with the monoclonal antibody and the N-terminally acetylated pentapeptide, Ac-Met-Asp-Pro-Asn-Cys-OH, was the smallest peptide which exhibited a significant reactivity with the antibody.