Designed 2D protein crystals as dynamic molecular gatekeepers for a solid-state device.
basic_science · Level V
Where this comes from
- Record sourced from PubMed, PMID 39068153.
- Also identified by DOI 10.1038/s41467-024-50567-8 and PMC identifier 11283500.
- Licence recorded as CC BY.
- The licence permits redistribution, so the abstract is shown in full and the full text is available from the publisher.
Abstract
The sensitivity and responsiveness of living cells to environmental changes are enabled by dynamic protein structures, inspiring efforts to construct artificial supramolecular protein assemblies. However, despite their sophisticated structures, designed protein assemblies have yet to be incorporated into macroscale devices for real-life applications. We report a 2D crystalline protein assembly of <sup>C98/E57/E66</sup>L-rhamnulose-1-phosphate aldolase (<sup>CEE</sup>RhuA) that selectively blocks or passes molecular species when exposed to a chemical trigger. <sup>CEE</sup>RhuA crystals are engineered via cobalt(II) coordination bonds to undergo a coherent conformational change from a closed state (pore dimensions <1 nm) to an ajar state (pore dimensions ~4 nm) when exposed to an HCN(g) trigger. When layered onto a mesoporous silicon (pSi) photonic crystal optical sensor configured to detect HCN<sub>(g)</sub>, the 2D <sup>CEE</sup>RhuA crystal layer effectively blocks interferents that would otherwise result in a false positive signal. The 2D <sup>CEE</sup>RhuA crystal layer opens in selective response to low-ppm levels of HCN<sub>(g)</sub>, allowing analyte penetration into the pSi sensor layer for detection. These findings illustrate that designed protein assemblies can function as dynamic components of solid-state devices in non-aqueous environments.
Medical subject headings
- Aldehyde-Lyases