Multivalent‐Interaction‐Driven Assembly of Discrete, Flexible, and Asymmetric Supramolecular Protein Nano‐Prisms

Abstract

Current approaches to design monodisperse protein assemblies require rigid, tight, and symmetric interactions between oligomeric protein units.H erein, we introduce an ew multivalent-interaction-driven assembly strategy that allows flexible,s paced, and asymmetric assembly between protein oligomers.Wediscoveredthat two polygonal protein oligomers (ranging from triangle to hexagon) dominantly form adiscrete and stable two-layered protein prism nanostructure via multivalent interactions between fused binding pairs.W ed emonstrated that protein nano-prisms with long flexible peptide linkers (over 80 amino acids) between protein oligomer layers could be discretely formed. Oligomers with different structures could also be monodispersely assembled into two-layered but asymmetric protein nano-prisms.F urthermore,p roducing higher-order architectures with multiple oligomer layers,f or example,3-layeredn ano-prisms or nanotubes,w as also feasible.

Biomolecular phase separation through theoretical and computational microscope

“…15,16 Since weak multivalent interactions between stickers are the primary driving forces of phase separation, it is crucial to comprehend the various modes of interactions that cause proteins to assemble and demix from their solvated state. 26,27 In the multi-domain proteins, various types of interactions collectively work to associate different sticker domains, while IDPs have a more well-defined list of interactions between amino acids playing a significant role in sticker-sticker interactions, which are discussed below. 28…”

Advances in Rational Protein Engineering toward Functional Architectures and Their Applications in Food Science

“…Assembly of the three-dimensional structures can be attributed to the delicate balance of multiple noncovalent interactions including electrostatic interactions, hydrogen bonds, hydrophobic interactions, π-stacking interactions, et al 18 Usually, complex interplays of polyvalence and the abundance of those biomolecular interactions define a final structure of the architecture as well as its functionality. 19 Although the underlying mechanism of the protein folding problem has yet to be fully solved, some significant rules on protein folding and assembly have been illustrated. Thus, the rational design of protein architectures requires a deep and comprehensive understanding of those interactions.…”