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Accession number;02A0304375
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| Title;Disintegration of .BETA.-Sheet Assemblage by Small Peptide that Lack Proton Donors. |
| Author;
YAMADA NORIHIRO
(Chiba Univ., Fac. of Educ.)
HANAMOTO KO
(Chiba Univ., Fac. of Educ.)
TAGAMI YUICHI
(Chiba Univ., Fac. of Educ.)
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Journal Title;Abstracts. Symposium on Biofunctional Chemistry
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Journal Code:L0836A
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ISSN:
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VOL.16th;NO.;PAGE.38-39(2001)
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| Figure&Table&Reference; |
| Pub. Country;Japan |
| Language;Japanese |
| Abstract;Amphiphilic molecules that contain a tripeptide moiety form an aggregate not only in water but also in organic solvents. The aggregate possesses fibrous morphology and involves a rich amount of parallel .BETA.-sheet structure of peptides, which is similar to a .BETA.-peptide called an amyloid fibril. These similarities suggest that the tripeptide-containing amphiphiles are suitable for an amyloid model. In the present study, we attempted to disintegrate the .BETA.-sheet assemblage by addition of a terminator molecule that lacked two proton donors for the interpeptide H-bonding. Aggregation of a tripeptide-containing amphiphile is accompanied by gel formation. The organogel turned into a light solution by addition of the terminator molecule. (author abst.) |
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