Drastic effects on fibril formation of amyloid-beta peptides by the addition of amino acid residue units to the termini.
We report that the addition of amino acids to the amyloid peptide dramatically affected the structure and the rate of formation of amyloid fibrils. The attachment of three lysines to Abeta(10-35) gave the formation of remarkably long fibrils, while three glutamates resulted in a faster formation rate of the fibrils.
Asanomi
Yuya
Y
Laboratory of Biological Chemistry, Department of Chemistry, Faculty of Science, Hokkaido University, N10, W8, Kita-ku, Sapporo 060-0810, Japan.
Kobayashi
Yumiko
Y
Sakai
Hiroki
H
Masuda
Takuya
T
Chen
Xinjiang
X
Chuman
Yoshiro
Y
Uosaki
Kohei
K
Sakaguchi
Kazuyasu
K
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000737:chemistry* / Q000378:metabolism; D016229:Amyloid beta-Peptides / Q000737:chemistry* / Q000378:metabolism; D018625:Microscopy, Atomic Force; D008969:Molecular Sequence Data; D055503:Protein Multimerization; D013329:Structure-Activity Relationship
D000596:Amino Acids; D016229:Amyloid beta-Peptides