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Journal of Biochemistry Advance Access published online on April 24, 2007
Journal of Biochemistry, doi:10.1093/jb/mvm099
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© 2007 The Japanese Biochemical Society

Marked difference between self-aggregations of first and fourth repeat peptides on tau microtubule-binding domain in acidic solution

Fumie Mizushima1, Katsuhiko Minoura1,{dagger}, Koji Tomoo1, Miho Sumida2, Taizo Taniguchi2 and Toshimasa Ishida1

1Osaka University of Pharmaceutical Sciences, 4-20-1 Nasahara, Takatsuki, Osaka 569-1094, Japan; and 2Behavioral and Medical Sciences Research Consortium, 2-5-7 Tamachi, Akashi, Hyogo 673-0025, Japan

{dagger}To whom correspondence should be addressed: Katsuhiko Minoura: E-mail: minoura{at}gly.oups.ac.jp

Received March 2, 2007; Accepted April 17, 2007


  Abstract

The heparin-induced self-aggregation behaviors 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 behaviors 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 behavior for filament formation. This is the first report on the markedly different self-aggregation behaviors of the first and fourth repeat peptides on tau microtubule-binding domain.

Key Words: tau, microtubule-binding domain, repeat peptide, filament formation, conformational transition


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