Marked difference between self-aggregations of first and fourth repeat peptides on tau microtubule-binding domain in acidic solution.
The heparin-induced self-aggregation behaviours of four repeat peptides (R1-R4) in an acidic solution (pH = 4.5) were investigated by fluorescence and circular dichroism (CD) measurements and compared with those in a neutral solution (pH = 7.5). In contrast with the self-aggregation-resistive behaviours of the R1 and R4 repeat peptides in the neutral solution, the R4 peptide formed a filament similarly to the R2 and R3 peptides in the acidic solution, whereas the R1 peptide still showed resistive behaviour for filament formation. This is the first report on the markedly different self-aggregation behaviours of the first and fourth repeat peptides on tau microtubule-binding domain.
Mizushima
Fumie
F
Osaka University of Pharmaceutical Sciences, 4-20-1 Nasahara, Takatsuki, Osaka 569-1094, Japan.
Minoura
Katsuhiko
K
Tomoo
Koji
K
Sumida
Miho
M
Taniguchi
Taizo
T
Ishida
Toshimasa
T
D000595:Amino Acid Sequence; D001665:Binding Sites; D002942:Circular Dichroism; D006493:Heparin / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D008854:Microscopy, Electron; D008870:Microtubules / Q000737:chemistry / Q000378:metabolism; D008969:Molecular Sequence Data; D010455:Peptides / Q000138:chemical synthesis / Q000737:chemistry* / Q000378:metabolism; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D020449:Repetitive Sequences, Amino Acid; D012996:Solutions / Q000378:metabolism; D013050:Spectrometry, Fluorescence; D013997:Time Factors; D016875:tau Proteins / Q000737:chemistry* / Q000378:metabolism
D010455:Peptides; D012996:Solutions; D016875:tau Proteins; D006493:Heparin