Amyloidogenic synthetic peptides of beta 2-microglobulin-a role of the disulfide bond

To search for the essential regions responsible for the beta 2-microglobulin ( beta 2-m) amyloid fibril formation, we synthesized six peptides corresponding to six of the seven beta -sheets in the native structure of beta 2-m, and examined their amyloidogenicity. Among the peptides examined, peptide...

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Bibliographic Details
Published in:Biochemical and biophysical research communications 2003-04, Vol.304 (1), p.101-106
Main Authors: Hasegawa, K, Ohhashi, Y, Yamaguchi, I, Takahashi, N, Tsutsumi, S, Goto, Y, Gejyo, F, Naiki, H
Format: Article
Language:English
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Summary:To search for the essential regions responsible for the beta 2-microglobulin ( beta 2-m) amyloid fibril formation, we synthesized six peptides corresponding to six of the seven beta -sheets in the native structure of beta 2-m, and examined their amyloidogenicity. Among the peptides examined, peptide (21-31) (strand B) and the mixture of peptide (21-31) and (78-86) (strand F) showed fibril formation at both pH 2.5 and 7.5. Peptide (21-31) is the N-terminal half of the previously reported proteolytic fragment of beta 2-m, Ser21-Lys41 (K3), suggesting that this region may be the essential core. Interestingly, the dimer formation of peptide (21-31) by the disulfide bond substantially facilitated the fibril formation, indicating that the disulfide bond is important for the structural stability of the fibrils.
ISSN:0006-291X
DOI:10.1016/S0006-291X(03)00543-6