Recognition-Driven Assembly of Self-Limiting Protein Supraparticles displaying Enzymatic Activity

PICCININI, ESTEBAN; DIEGO PALLAROLA; BATTAGLINI, FERNANDO; AZZARONI, OMAR

Viena

Workshop; Bioelectrochemistry and more 2016; 2016

CEST

Self-assembled colloidal nanoparticles is of paramount relevance for opening new research frontiers in nanoscience and nanotechnology for a wide range of biological and chemical systems.1 Recent progress has been made in developing nature-inspired strategies for the synthesis of self-associated hybrid particles combining organic, bio and inorganic components.2 The synthetic efforts have been focused on the creation of functional structures that combine not only properties of the individual components but also exploit the interactions between constituting particles in a synergetic manner.3 Progress in this field aims to systems with increased complexity where specific functionalities can be introduced and displayed in a simple but efficient fashion. To perform specific functions, use of proteins, or more precisely: enzymes, as building blocks is an attractive approach owing to their inherent structural and chemical properties.4 Yet, it is still a challenging task to create protein-based programmable suprastructures with controlled size uniformity and composition by simple harnessing these interactions. In this work, we demonstrate that under specific conditions, the assembly between a ligand-binding protein (Concanavalin A, Con A) and a ligand-presenting enzyme (Glucose oxidase, GOx) proceeds through a self-limited growth process.5 The balance between attractive and repulsive interactions leads to bionanoparticles (BNPs) with defined size and composition. The as-synthesized BNPs retain the enzymatic activity and exhibited enhanced ligand-binding affinity. Moreover, the supraparticles were successfully assembled on gold surfaces functionalized with mannose residues. Then, multilayer interfacial architectures were constructed by sequential assembly of biosupraparticles and concanavalin A on electrode surfaces. These results suggest that the biocolloids act as ambivalent recognition particles, which bind both to mannose and concanavalin A with high affinity.[1] B. Pelaz, S. Jaber, D. J. De Aberasturi, V. Wulf, T. Aida, J. M. De La Fuente, J. Feldmann, H. E. Gaub, L. Josephson, C. R. Kagan, N. Kotov, L. M. Liz-Marzán, H. Mattoussi, P. Mulvaney, C. B. Murray, A. L. Rogach, P. S. Weiss, I. Willner and W. J. Parak, ACS Nano, 2012, 6, 8468?8483.[2] E. Piccinini, D. Pallarola, F. Battaglini, O. Azzaroni, Mol. Syst. Des. Eng., 2016.[3] J. Il Park, T. D. Nguyen, G. de Queirós Silveira, J. H. Bahng, S. Srivastava, G. Zhao, K. Sun, P. Zhang, S. C. Glotzer and N. Kotov, Nat. Commun., 2014, 5, 3593.[4] K. Ariga, Q. Ji, T. Mori, M. Naito, Y. Yamauchi, H. Abe and J. P. Hill, Chem. Soc. Rev., 2013, 42, 6322?6345.[5] E. Piccinini, D. Pallarola, F. Battaglini and O. Azzaroni, Chem. Commun., 2015, 51, 14754?14757.