Cross-linking of a synthetic partial-length (1-28) peptide of the Alzheimer beta/A4 amyloid protein by transglutaminase.

Abstract:

:Cerebral deposits of beta/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.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Ikura K,Takahata K,Sasaki R

doi

10.1016/0014-5793(93)81772-r

subject

Has Abstract

pub_date

1993-07-12 00:00:00

pages

109-11

issue

1-3

eissn

0014-5793

issn

1873-3468

pii

0014-5793(93)81772-R

journal_volume

326

pub_type

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