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Journal of Biochemistry Advance Access originally published online on April 24, 2007
Journal of Biochemistry 2007 142(1):49-54; 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,*, Koji Tomoo1, Miho Sumida2, Taizo Taniguchi2 and Toshimasa Ishida1

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

*To whom correspondence should be addressed. Tel: 072-690-1068, Fax: 072-690-1068, E-mail: minoura{at}gly.oups.ac.jp

Received March 2, 2007; Accepted April 17, 2007


  Abstract

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.

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

Abbreviations: AD, Alzheimer's disease; CD, circular dichroism; His, histidine; MBD, microtubule-binding domain; HPLC, high pressure liquid chromatography; 3RMBD, three-repeated MBD; 4RMBD, four-repeated MBD; MT, microtubule; PHF, paired helical filament; ThS, thioflavin S


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