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

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Abstract
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