pH-responsive self-assembly of amyloid fibrils for dual hydrolase-oxidase reactions
Díaz-Caballero, Marta (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí")
Navarro, Susanna (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular)
Nuez-Martínez, Miquel (Institut de Ciència de Materials de Barcelona)
Peccati, Francesca (Basque Research and Technology Alliance)
Rodríguez Santiago, Luis (Universitat Autònoma de Barcelona. Departament de Química)
Sodupe Roure, Mariona (Universitat Autònoma de Barcelona. Departament de Química)
Teixidor, Francesc (Institut de Ciència de Materials de Barcelona)
Ventura, Salvador (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí")

Fecha:	2021
Resumen:	There is an increasing interest in synthetic systems that can execute bioinspired chemical reactions without requiring the complex structures that characterize enzymes in their components. The hierarchical self-assembly of peptides provides a means to create catalytic microenvironments. Ideally, as it occurs in enzymes, the catalytic activity of peptide nanostructures should be reversibly regulated. In a typical enzyme mimetic design, the peptide's self-assembling and catalytic activities are segregated into different regions of the sequence. Here, we aimed to design minimal peptides in which the self-assembly and function were all encoded in the same amino acids. Moreover, we wanted to endow the resulting one-component nanomaterial with divergent, chemically unrelated, catalytic activities, a property not observed in natural enzymes. We show that short peptides consisting only of histidine and tyrosine residues, arranged in a binary pattern, form biocompatible amyloid-like fibrils and hydrogels combining hydrolytic and electrocatalytic activities. The nanofibers' mesoscopic properties are controlled by pH, the transition between assembled active β-sheet fibrils, and disassembled inactive random coil species occurring in a physiologically relevant pH range. The structure of one of such amyloid-like fibrils, as derived from molecular dynamic simulations, provides insights on how they attain this combination of structural and catalytic properties.
Ayudas:	Ministerio de Economía y Competitividad BFU2013-44763-P Ministerio de Economía y Competitividad BIO2016-78310-R Ministerio de Educación, Cultura y Deporte FPU14/05786 Agencia Estatal de Investigación CTQ2017-89132-P Agència de Gestió d'Ajuts Universitaris i de Recerca 2017/SGR-1323
Nota:	Altres ajuts: ICREA Academia 2015
Derechos:	Tots els drets reservats.
Lengua:	Anglès
Documento:	Article ; recerca ; Versió acceptada per publicar
Materia:	Amyloid fibrils ; Artificial enzymes ; Hydrogels ; Ph-responsive materials ; Self-assembly ; Short peptides
Publicado en:	ACS catalysis, Vol. 11, Issue 2 (January 2021) , p. 595-607, ISSN 2155-5435

DOI: 10.1021/acscatal.0c03093

Postprint 47 p, 5.4 MB

El registro aparece en las colecciones:
Documentos de investigación > Documentos de los grupos de investigación de la UAB > Centros y grupos de investigación (producción científica) > Ciencias de la salud y biociencias > Instituto de Biotecnología y de Biomedicina (IBB)
Artículos > Artículos de investigación
Artículos > Artículos publicados