TY  - JOUR
AU  - Rütten, Michael
AU  - Lang, Laurin
AU  - Wagler, Henrike
AU  - Lach, Marcel
AU  - Mucke, Niklas
AU  - Laugks, Ulrike
AU  - Seuring, Carolin
AU  - Keller, Thomas F.
AU  - Stierle, Andreas
AU  - Ginn, Helen M.
AU  - Beck, Tobias
TI  - Assembly of Differently Sized Supercharged Protein Nanocages into Superlattices for Construction of Binary Nanoparticle–Protein Materials
JO  - ACS nano
VL  - 18
IS  - 36
SN  - 1936-0851
CY  - Washington, DC
PB  - Soc.
M1  - PUBDB-2024-06074
SP  - 25325-25336
PY  - 2024
AB  - This study focuses on the design and characterization of binary nanoparticle superlattices: Two differently sized, supercharged protein nanocages are used to create a matrix for nanoparticle arrangement. We have previously established the assembly of protein nanocages of the same size. Here, we present another approach for multicomponent biohybrid material synthesis by successfully assembling two differently sized supercharged protein nanocages with different symmetries. Typically, the ordered assembly of objects with nonmatching symmetry is challenging, but our electrostatic-based approach overcomes the symmetry mismatch by exploiting electrostatic interactions between oppositely charged cages. Moreover, our study showcases the use of nanoparticles as a contrast enhancer in an elegant way to gain insights into the structural details of crystalline biohybrid materials. The assembled materials were characterized with various methods, including transmission electron microscopy (TEM) and single-crystal small-angle X-ray diffraction (SC-SAXD). We employed cryo-plasma-focused ion beam milling (cryo-PFIB) to prepare lamellae for the investigation of nanoparticle sublattices via electron cryo-tomography. Importantly, we refined superlattice structure data obtained from single-crystal SAXD experiments, providing conclusive evidence of the final assembly type. Our findings highlight the versatility of protein nanocages for creating distinctive types of binary superlattices. Because the nanoparticles do not influence the type of assembly, protein cage matrices can combine various nanoparticles in the solid state. This study not only contributes to the expanding repertoire of nanoparticle assembly methods but also demonstrates the power of advanced characterization techniques in elucidating the structural intricacies of these biohybrid materials.
LB  - PUB:(DE-HGF)16
C6  - pmid:39189351
UR  - <Go to ISI:>//WOS:001300237000001
DO  - DOI:10.1021/acsnano.4c09551
UR  - https://bib-pubdb1.desy.de/record/615179
ER  -