Site-specific amino acid D-isomerization of Tau R2 and R3 peptides changes the fibril morphology, resulting in attenuation of Tau aggregation inhibitor potency.

Murata, Takuya; Ito, Genta; Utsunomiya-Tate, Naoko

Murata, Takuya; Ito, Genta; Utsunomiya-Tate, Naoko.

Afiliação

Murata T; Department of Biomolecular Chemistry, Faculty of Pharmaceutical Sciences, Teikyo University, 2-11-1, Kaga, Itabashi-ku, Tokyo, 173-8605, Japan.
Ito G; Department of Biomolecular Chemistry, Faculty of Pharmaceutical Sciences, Teikyo University, 2-11-1, Kaga, Itabashi-ku, Tokyo, 173-8605, Japan.
Utsunomiya-Tate N; Department of Biomolecular Chemistry, Faculty of Pharmaceutical Sciences, Teikyo University, 2-11-1, Kaga, Itabashi-ku, Tokyo, 173-8605, Japan. Electronic address: tate@pharm.teikyo-u.ac.jp.

Biochem Biophys Res Commun ; 654: 18-25, 2023 04 30.

Article em En | MEDLINE | ID: mdl-36878036

Assuntos

Doença de Alzheimer; Humanos; Doença de Alzheimer/metabolismo; Aminoácidos; Sequência de Aminoácidos; Proteínas tau/metabolismo; Isomerismo; Peptídeos/química

Palavras-chave

Aggregation inhibitor; D-isomerization; Fibril morphology; Microtubule-binding repeat domain; Tau

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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Doença de Alzheimer Limite: Humans Idioma: En Ano de publicação: 2023 Tipo de documento: Article

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