Lyophilization of biomimetic amyloids preserves their regulatable, endocrine-like functions for nanoparticle release
de Pinho Favaro, Marianna T. (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí")
López-Laguna, Hèctor (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí")
Voltà-Durán, Eric (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí")
Alba Castellón, Lorena (Institut de Recerca Sant Pau)
Sanchez, Julieta M. (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí")
Casanova Rigat, Isolda (Institut de Recerca Sant Pau)
Unzueta Elorza, Ugutz (Institut de Recerca Sant Pau)
Mangues, Ramon 1957- (Institut Germans Trias i Pujol. Institut de Recerca contra la Leucèmia Josep Carreras)
Villaverde Corrales, Antonio (Universitat Autònoma de Barcelona. Departament de Genètica i de Microbiologia)
Vázquez Gómez, Esther (Universitat Autònoma de Barcelona. Departament de Genètica i de Microbiologia)

Date:	2024
Abstract:	The secretory granules from the mammalian endocrine system are functional amyloids that act as dynamic depots to store and release protein hormones into the bloodstream. The controlled in vitro coordination between divalent cations and solvent-exposed histidine residues triggers reversible, cross-molecular interactions that result in granular protein aggregates with protein-leaking properties. While these synthetic particles are mechanically stable, they progressively disintegrate and release their protein building blocks, mimicking the performance of secretory granules. Envisaged as delivery systems for endocrine-like, time-sustained protein release, their clinical applicability should be supported by robust storage procedures, so far unset. Being lyophilization a desirable storage method for protein drugs, how this procedure could preserve the performance of clinically oriented functional amyloids is a neglected issue. We have here explored, tailored and validated lyophilization as an industrially and clinically friendly, fully scalable approach to the storage of functional amyloids aimed at secretion of protein-only nanoparticles. By doing so, protein-protein interactions in such materials have been characterized, and citrate identified as an efficient modulator of the temporal secretion profile, through which the sustainability of the leaking process can be finely regulated.
Grants:	Agencia Estatal de Investigación PID2019-105416RB-I00 Agencia Estatal de Investigación PDC2022-133858-I00 Agencia Estatal de Investigación PID2022-1368450-OB-10 Instituto de Salud Carlos III PI20/00400 Instituto de Salud Carlos III PI23/00318 Instituto de Salud Carlos III PI21/00150 Agència de Gestió d'Ajuts Universitaris i de Recerca 2021/SGR-00092 Agència de Gestió d'Ajuts Universitaris i de Recerca 2021/SGR-01140 Ministerio de Sanidad y Consumo CB06/01/0014 Instituto de Salud Carlos III CB06/01/1031 Instituto de Salud Carlos III CP19/00028
Note:	Altres ajuts: acords transformatius de la UAB
Rights:	Aquest document està subjecte a una llicència d'ús Creative Commons. Es permet la reproducció total o parcial, la distribució, la comunicació pública de l'obra i la creació d'obres derivades, sempre que no sigui amb finalitats comercials, i sempre que es reconegui l'autoria de l'obra original.
Language:	Anglès
Document:	Article ; recerca ; Versió publicada
Subject:	Functional amyloids ; Recombinant proteins ; Dynamic protein depots ; Endocrine-like function ; Drug delivery
Published in:	Applied materials today, Vol. 39 (August 2024) , art. 102348, ISSN 2352-9407

DOI: 10.1016/j.apmt.2024.102348

14 p, 7.5 MB

The record appears in these collections:
Research literature > UAB research groups literature > Research Centres and Groups (research output) > Health sciences and biosciences > Institut d'Investigació en Ciencies de la Salut Germans Trias i Pujol (IGTP) > Josep Carreras Leukaemia Research Institute
Research literature > UAB research groups literature > Research Centres and Groups (research output) > Health sciences and biosciences > Institut de Biotecnologia i de Biomedicina (IBB)
Articles > Research articles
Articles > Published articles