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Biotechnological applications of amyloid fibrils.
Nabi Afjadi, Mohsen; Aziziyan, Fatemeh; Farzam, Farnoosh; Dabirmanesh, Bahareh.
Afiliação
  • Nabi Afjadi M; Department of Biochemistry, Faculty of Biological Sciences, Tarbiat Modares University, Tehran, Iran.
  • Aziziyan F; Department of Biochemistry, Faculty of Biological Sciences, Tarbiat Modares University, Tehran, Iran.
  • Farzam F; Department of Biochemistry, Faculty of Biological Sciences, Tarbiat Modares University, Tehran, Iran.
  • Dabirmanesh B; Department of Biochemistry, Faculty of Biological Sciences, Tarbiat Modares University, Tehran, Iran. Electronic address: dabirmanesh@modares.ac.ir.
Prog Mol Biol Transl Sci ; 206: 435-472, 2024.
Article em En | MEDLINE | ID: mdl-38811087
ABSTRACT
Protein aggregates and amyloid fibrils have special qualities and are used in a variety of biotechnological applications. They are extensively employed in bioremediation, biomaterials, and biocatalysis. Because of their capacity to encapsulate and release pharmaceuticals and their sensitivity to certain molecules, respectively, they are also used in drug delivery and biosensor applications. They have also demonstrated potential in the domains of food and bioremediation. Additionally, amyloid peptides have drawn interest in biological applications, especially in the investigation of illnesses like Parkinson's and Alzheimer's. The unique characteristics of amyloid fibrils, namely their mechanical strength and ß-sheet structure, make them adaptable to a wide range of biotechnological uses. Even with their promise, one important factor to keep in mind before widely using modified amyloid materials is their potential toxicity. Thus, current research aims to overcome safety concerns while maximizing their potential.
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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Biotecnologia / Amiloide Limite: Animals / Humans Idioma: En Revista: Prog Mol Biol Transl Sci Assunto da revista: BIOLOGIA MOLECULAR Ano de publicação: 2024 Tipo de documento: Article País de afiliação: Irã

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Biotecnologia / Amiloide Limite: Animals / Humans Idioma: En Revista: Prog Mol Biol Transl Sci Assunto da revista: BIOLOGIA MOLECULAR Ano de publicação: 2024 Tipo de documento: Article País de afiliação: Irã