K. Ikura et al., CROSS-LINKING OF A SYNTHETIC PARTIAL-LENGTH (1-28) PEPTIDE OF THE ALZHEIMER BETA A4 AMYLOID PROTEIN BY TRANSGLUTAMINASE/, FEBS letters, 326(1-3), 1993, pp. 109-111
Cerebral deposits of beta/A4 amyloid protein is a pathologic sign of A
lzheimer's disease. A synthetic partial-length (1-28) peptide of this
protein contains one glutamine and two lysine residues. Here we show t
hat this peptide can be a substrate of transglutaminase, which catalyz
es 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 synt
hetic peptide was also cross-linked, but another modified version (Lys
16 to L-norleucine) was very poorly cross-linked, indicating that Lys1
6 is involved exclusively in the cross-linking of the partial-length p
eptide catalyzed by transglutaminase.