Amyloidogenic synthetic peptides of beta2-microglobulin--a role of the disulfide bond

To search for the essential regions responsible for the beta2-microglobulin (beta2-m) amyloid fibril formation, we synthesized six peptides corresponding to six of the seven beta-sheets in the native structure of beta2-m, and examined their amyloidogenicity. Among the peptides examined, peptide (21-...

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Veröffentlicht in:Biochemical and biophysical research communications 2003-04, Vol.304 (1), p.101-106
Hauptverfasser: Hasegawa, Kazuhiro, Ohhashi, Yumiko, Yamaguchi, Itaru, Takahashi, Naoki, Tsutsumi, Shinobu, Goto, Yuji, Gejyo, Fumitake, Naiki, Hironobu
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container_title Biochemical and biophysical research communications
container_volume 304
creator Hasegawa, Kazuhiro
Ohhashi, Yumiko
Yamaguchi, Itaru
Takahashi, Naoki
Tsutsumi, Shinobu
Goto, Yuji
Gejyo, Fumitake
Naiki, Hironobu
description To search for the essential regions responsible for the beta2-microglobulin (beta2-m) amyloid fibril formation, we synthesized six peptides corresponding to six of the seven beta-sheets in the native structure of beta2-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 beta2-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.
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subjects Amino Acid Sequence
Amyloid - chemistry
Amyloid - ultrastructure
beta 2-Microglobulin - chemistry
Chromatography, High Pressure Liquid
Disulfides - chemistry
Dithiothreitol - pharmacology
Kinetics
Molecular Sequence Data
Peptides - chemistry
Protein Structure, Secondary
Sequence Deletion
title Amyloidogenic synthetic peptides of beta2-microglobulin--a role of the disulfide bond
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