The spectrum of building block conformers sustains the biophysical properties of clinically-oriented self-assembling protein nanoparticles

作     者：Eric Voltà-Durán Julieta M Sánchez Hèctor-López-Laguna Eloi Parladé Laura Sánchez-García Alejandro Sánchez-Chardi Ario de Marco Ugutz Unzueta Esther Vázquez Antonio Villaverde Eric Voltà-Durán;Julieta M Sánchez;Hèctor-López-Laguna;Eloi Parladé;Laura Sánchez-García;Alejandro Sánchez-Chardi;Ario de Marco;Ugutz Unzueta;Esther Vázquez;Antonio Villaverde

作者机构：Institut de Biotecnologia i de BiomedicinaUniversitat Autònoma de BarcelonaBellaterra 08193BarcelonaSpain Departament de Genètica i de MicrobiologiaUniversitat Autònoma de BarcelonaBellaterra 08193BarcelonaSpain CIBER de Bioingeniería Biomateriales y Nanomedicina(CIBER-BBN)Bellaterra 08193BarcelonaSpain Instituto de Investigaciones Biológicas y Tecnológicas(IIBYT)(CONICET-Universidad Nacional de Córdoba)ICTA&Cátedra de Química BiológicaDepartamento de QuímicaFCEFyNUNC.Av.Velez Sarsfield 1611X 5016GCA CórdobaArgentina Servei de MicroscòpiaUniversitat Autònoma de BarcelonaBellaterra 08193BarcelonaSpain Departament de Biologia EvolutivaEcologia i Ciències AmbientalsFacultat de BiologiaUniversitat de Barcelona08028 BarcelonaSpain Laboratory for Environmental and Life SciencesUniversity of Nova GoricaNova Gorica 5000Slovenia Biomedical Research Institute Sant Pau(IIB Sant Pau)Sant Antoni Ma Claret 16708025 BarcelonaSpain 

出 版 物：《Science China Materials》 (中国科学（材料科学（英文版）)

年 卷 期：2022年第65卷第6期

页      面：1662-1670页

核心收录：

学科分类：071011[理学-生物物理学] 0710[理学-生物学] 07[理学] 070205[理学-凝聚态物理] 08[工学] 080501[工学-材料物理与化学] 0805[工学-材料科学与工程（可授工学、理学学位）] 0702[理学-物理学] 

基　　金：The AGAUR(2017SGR229)and the CIBER-BBN(project NANOPROTHER)are granted to Villaverde A.Vázquez E received support from the AEI(PID2019-105416RB-I00/AEI/10.13039/501100011033 and CIBER-BBN(project NANOREMOTE) support from the Javna Agencija za Raziskovalno dejavnost Republike Slovenije(ARRS/N4-0046 and ARRS/J4-9322)to de Marco A supported by a predoctoral fellowship from the AGAUR(2018FI_B2_00051) by a predoctoral fellowship from Ministerio de Ciencia,Innovacion y Universidades(FPU18/04615) supported by Miguel Servet contract(CP19/00028)from ISCIII co-funded by European Social Fund(ESF investing in your future) by an ISCIII project(PI20/00400)co-funding FEDER(A way to make Europe) supported by a predoctoral fellowship from the AGAUR(2019FI_B00352) support from NIH P41GM103311 

主　　题：recombinant proteins self-assembling protein materials nanoparticles biomaterials 

摘      要：Histidine-rich peptides confer self-assembling properties to recombinant proteins through the supramolecular coordination with divalent *** fact allows the cost-effective,large-scale generation of microscopic and macroscopic protein materials with intriguing biomedical *** such materials,resulting from the simple bioproduction of protein building blocks,homomeric nanoparticles are of special value as multivalent interactors and drug ***,we have here identified that the assembly of a given His-tagged protein might render distinguishable categories of self-assembling protein *** fact has been scrutinized through the nanobody-containing fusion proteins EM1-GFP-H6 and A3C8-GFP-H6,whose biosynthesis results in two distinguishable populations of building *** one of them,the assembling and disassembling is controllable by ***,a second population immediately self-assembles upon purification through a non-regulatable pathway,rendering larger nanoparticles with specific biological *** structural analyses of both model proteins and nanoparticles revealed important conformational variability in the building *** fact renders different structural and functional categories of the final soft materials resulting from the participation of energetically unstable intermediates in the oligomerization *** data illustrate the complexity of the Hismediated protein assembling in recombinant proteins but they also offer clues for a better design and refinement of protein-based nanomedicines,which,resulting from biological fabrication,show an architectonic flexibility unusual among biomaterials.