Journal
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
Volume 22, Issue 2, Pages -Publisher
MDPI
DOI: 10.3390/ijms22020812
Keywords
peptides; beta-2-Microglobulin; DNA; atomic force microscopy (AFM); computational design; self-assembly; biosensor
Funding
- ERC Advanced Grant MoNaLiSA: QUIDPROQUO [269025]
- Associazione Italiana per la Ricerca sul Cancro (AIRC) [12214, 18510]
- Italian Ministry of Health [WFR GR-2013-02356714]
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The study introduces a rationally designed nanochip capable of capturing a target protein using computationally evolved peptides. Through nanopatterning the surface, the study successfully controlled the specific capture of peptides for the protein, demonstrating the feasibility of this approach in peptide design.
The bottom-up design of smart nanodevices largely depends on the accuracy by which each of the inherent nanometric components can be functionally designed with predictive methods. Here, we present a rationally designed, self-assembled nanochip capable of capturing a target protein by means of pre-selected binding sites. The sensing elements comprise computationally evolved peptides, designed to target an arbitrarily selected binding site on the surface of beta-2-Microglobulin (beta 2m), a globular protein that lacks well-defined pockets. The nanopatterned surface was generated by an atomic force microscopy (AFM)-based, tip force-driven nanolithography technique termed nanografting to construct laterally confined self-assembled nanopatches of single stranded (ss)DNA. These were subsequently associated with an ssDNA-peptide conjugate by means of DNA-directed immobilization, therefore allowing control of the peptide's spatial orientation. We characterized the sensitivity of such peptide-containing systems against beta 2m in solution by means of AFM-based differential topographic imaging and surface plasmon resonance (SPR) spectroscopy. Our results show that the confined peptides are capable of specifically capturing beta 2m from the surface-liquid interface with micromolar affinity, hence providing a viable proof-of-concept for our approach to peptide design.
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