Amino Acids and Peptides. XIII. : Synthesis of a Nonacosapeptide Corresponding to the N-Terminal Sequence 1-29 (β-Fragment) of Human Liver Metallothionein II (hMT II) and Its Heavy Metal-Binding Properties

• Published in: Chemical & pharmaceutical bulletin Vol. 34; no. 3; pp. 986 - 998
• Main Authors: OKADA, YOSHIO, OHTA, NORIYA, IGUCHI, SHIN, TSUDA, YUKO, SASAKI, HIDEAKI, KITAGAWA, TOKUJIRO, YAGYU, MASAMI, MIN, KYON-SON, ONOSAKA, SATOMI, TANAKA, KEIICHI
• Format: Journal Article
• Language: English
• Published: Tokyo The Pharmaceutical Society of Japan 1986; Maruzen
• Subjects: Amino Acid Sequence; Chemistry; Exact sciences and technology; heavy metal-binding property; Humans; liver; Liver - analysis; man; metallothionein; Metallothionein - chemical synthesis; Metallothionein - metabolism; Metals - metabolism; Organic chemistry; peptide synthesis; Peptides; Preparations and properties; Protein Binding; Liquid phase; Oligopeptides; Peptide fragment; Peptidic synthesis
• ISSN: 0009-2363; 1347-5223
• DOI: 10.1248/cpb.34.986

A nonacosapeptide corresponding to the N-terminal sequence 1-29 (β-fragment) of human liver metallothionein II (hMT II) was synthesized by the azide coupling of five peptide fragments [1, 2, 4, 6 and 8], followed by HF deprotection and its heavy metal-binding properties were examined. It was revealed that the Cd-binding ability of the synthetic β-fragment as well as synthetic α-fragment corresponding to the C-terminal sequence 30-61 of hMT II was stronger than that of native rat thionein. Moreover, it was found that both the α-and β-fragments bound preferentially to Cu ions rather than Cd ions.