Issue 24, 2021

Measuring interactions of DNA with nanoporous protein crystals by atomic force microscopy

Abstract

Crosslinked porous protein crystals are a new biomaterial that can be engineered to encapsulate, stabilize, and organize guest molecules, nanoparticles, and biological moieties. In this study, for the first time, the combined interactions of DNA strands with porous protein crystals are quantitatively measured by high-resolution atomic force microscopy (AFM) and chemical force microscopy. The surface structure of protein crystals with unusually large pores was observed in liquid via high-resolution AFM. Force–distance (FD) curves were also obtained using AFM tips modified to present or capture DNA. The modification of AFM tips allowed the tips to covalently bind DNA that was pre-loaded in the protein crystal nanopores. The modified tips enabled the interactions of DNA molecules with protein crystals to be quantitatively studied while revealing the morphology of the buffer-immersed protein crystal surface in detail, thereby preserving the structure and properties of protein crystals that could be disrupted or destroyed by drying. The hexagonal space group was manifest at the crystal surface, as were the strong interactions between DNA and the porous protein crystals in question. In sum, this study furthered our understanding of how a new protein-based biomaterial can be used to bind guest DNA assemblies.

Graphical abstract: Measuring interactions of DNA with nanoporous protein crystals by atomic force microscopy

Supplementary files

Article information

Article type
Paper
Submitted
17 Mar 2021
Accepted
03 Jun 2021
First published
09 Jun 2021

Nanoscale, 2021,13, 10871-10881

Author version available

Measuring interactions of DNA with nanoporous protein crystals by atomic force microscopy

D. Wang, J. D. Stuart, A. A. Jones, C. D. Snow and M. J. Kipper, Nanoscale, 2021, 13, 10871 DOI: 10.1039/D1NR01703A

To request permission to reproduce material from this article, please go to the Copyright Clearance Center request page.

If you are an author contributing to an RSC publication, you do not need to request permission provided correct acknowledgement is given.

If you are the author of this article, you do not need to request permission to reproduce figures and diagrams provided correct acknowledgement is given. If you want to reproduce the whole article in a third-party publication (excluding your thesis/dissertation for which permission is not required) please go to the Copyright Clearance Center request page.

Read more about how to correctly acknowledge RSC content.

Social activity

Spotlight

Advertisements