Cross‐linking of a synthetic partial‐length (1–28) peptide of the Alzheimer β/A4 amyloid protein by transglutaminase

FEBS Letters

Ikura, Koji³  Sasaki, Ryuzo²  Takahata, Kyoya¹ 

[1] Department of Bioresources Chemistry, Okayama University, Okayama 700, Japan;Department of Food Science and Technology, Kyoto University, Kyoto 606-01, Japan;Department of Chemistry and Materials Technology, Kyoto Institute of Technology, Kyoto 606, Japan

关键词: Transglutaminase;    Amyloid beta-protein;    Alzheimer's disease;   

DOI  :  10.1016/0014-5793(93)81772-R

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Cerebral deposits of β/A4 amyloid protein is a pathologic sign of Alzheimer's disease. A synthetic partial-length (1–28) peptide of this protein contains one glutamine and two lysine residues. Here we show that this peptide can be a substrate of transglutaminase, which catalyzes cross-linking between glutamine and lysine residues in peptides, by demonstrating the formation of multimeric peptides due to the action of this enzyme. A modified (LyS²⁸ to l-norleucine) version of the synthetic peptide was also cross-linked, but another modified version (Lys¹⁶ to l-norleucine) was very poorly cross-linked, indicating that Lys¹⁶ is involved exclusively in the cross-linking of the partial-length peptide catalyzed by transglutaminase.

【 授权许可】

Unknown