Two-dimensional regular arrays of functional molecules like rotors represent a unique class of stimuli-responsive materials with exciting properties. Scientists led by <a href="https://kaleta.group.uochb.cz/en">Jiří Kaleta</a> from IOCB Prague in collaboration with colleagues from the University of Colorado, and the University of Oxford prepared an array composed of a unique type of fullerene-based molecular rotors with a relatively high dipole moment.
<img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/UOCHB_Surface_mounted_regular_arrays_of_fullerene_based_molecular_rotors_cover_image_acde0c0f48.jpg" alt="IOCB Prague: Surface-mounted regular arrays of fullerene-based molecular rotors - cover image"/>
The scientists successfully inserted these rotors into a porous zeolite-like matrix and characterized the surface inclusions by transmission electron microscopy (TEM), powder X-ray diffraction (PXRD), and solid-state NMR techniques. They have found that half of the guest rotors is immersed relatively deeply into the matrix, while the other half shallowly. This resulted in different fullerene rotation barriers due to a different chemical environment based on the different rotor penetration depth.
The study was highlighted in <a href="https://pubs.rsc.org/en/journals/articlecollectionlanding?sercode=cc&amp;themeid=c05977e6-28fb-43a9-b5e4-5954d33bd6c8">Chemical Communications HOT Articles 2024</a>.
<img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/UOCHB_Chemical_Communications_Surface_mounted_regular_arrays_of_fullerene_based_molecular_rotors_96d6a8cf63.jpg" alt="IOCB Prague/Chemical Communications: Surface-mounted regular arrays of fullerene-based molecular rotors"/>
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Surface-mounted regular arrays of fullerene-based molecular rotors

The two most common folded protein secondary structure motifs are α-helices and β-sheets. Certain peptide sequences, some of them as short as amino acid triplets, are significantly overpopulated in α-helices motifs, and almost non-existent in the extended parts of proteins. In contrast, other triplets appear almost exclusively in extended parts represented typically by β-sheets.
A multidisciplinary research team led by <a href="https://rulisek.group.uochb.cz/en">Lubomír Rulíšek</a> and <a href="https://nmr.group.uochb.cz/en">Martin Dračínský</a> from <a href="https://icpms.labrulez.com/companies/62">IOCB Prague</a> wanted to determine whether such preferences are structurally encoded in a particular peptide fragment or appear only at the level of a complex protein structure.
The scientists identified several tripeptides, which could be considered as folding seeds and might initiate the process of protein folding. This has been indicated by VCD, ECD, and NMR spectroscopies and is fully supported by the quantum chemical calculations.
Surprisingly, only in a few cases was the folding preference of a standalone tripeptide same as its behavior in proteins. The presented results may indicate that the secondary structure starts to appear somewhere between 3 and 11 amino acid-long peptide sequences.

What are the minimal folding seeds in proteins?

Researchers led by Eliška Procházková from <a href="https://icpms.labrulez.com/companies/62">IOCB Prague</a> have found that azopyrimidine photoswitches become encapsulated into β-cyclodextrin (CD) cavity selectively via their phenyl ring. The strength of the complex is tuned by structural modification of azopyrimidine.
In the strongest complexes, the trans-to-cis isomerization proceeds inside the CD cavity. In the weak complexes, azopyrimidine in the trans isomer is complexed via the narrower primary portal and released from the CD cavity upon irradiation. Consequently, the resulting cis isomer is re-complexed through the wider secondary portal. 
This research highlights the applicability of these and similar types of supramolecular assemblies as a function of the interaction strength and mutual orientation of host and guest molecules, which have been studied for the first time in cases of cyclodextrin-azenyl couples by a combined NMR spectroscopy-capillary electrophoresis-quantum chemistry approach.

Azopyrimidine photoswitches and their interactions with cyclodextrins

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The Institute of Organic Chemistry and Biochemistry of the Czech Academy of Sciences (IOCB Prague) is a leading scientific institution in the Czech Republic, recognized internationally. Its primary mission is basic research in the fields of chemical biology and medicinal chemistry, organic and material oriented chemistry, chemistry of natural compounds, biochemistry and molecular biology, physical chemistry, theoretical chemistry, and analytical chemistry. 

Institute of Organic Chemistry and Biochemistry of the Czech Academy of Sciences

Azopyrimidine photoswitches and their interactions with cyclodextrins

What are the minimal folding seeds in proteins?

Surface-mounted regular arrays of fullerene-based molecular rotors

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