Ulijn Group, 2020

Welcome to the Ulijn Group website. Our lab is focused on the use of simple versions of the molecular building blocks of life to produce materials and systems with controllable structural, photonic, electronic, and biological properties. These properties open up wide-ranging applications in energy, biomedicine, environmental protection, food, cosmetics, and personal care. [Group Members and Full Biography]

Group News

We Are Recruiting!

@asrc_gc is seeking to recruit two highly motivated postdoctoral scholars to research systems-based design of biomolecular modalities and materials. Researchers who have experience or interests that bridge computation/theory and experiment are especially encouraged to consider these positions.

Come and join us in NYC! Apply here.

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Publication Spotlight

Expanding the Conformational Landscape of Minimalistic Tripeptides by Their O-Glycosylation

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Glycosylation is a common biological post-synthetic modification significant, yet under-explored implications for enhancing functionality in designed supramolecular materials. In this JACS publication, we use simple self-assembling tripeptides containing polar amino acids Ser and Thr as sites for glycosylation. Striking observations from the computational modeling of these systems show that the conformational landscape of these simple tripeptides, typically pre-organized by F-F self-stacking interactions, is dramatically increased by glycosylation. This is underpinned by the generation of a diverse supramolecular interactome consisting of contributions from weaker interactions such as CH-π. We also find striking and counter-intuitive differences between the two-polar amino acids studied, with the more hydrophobic Thr residue causing an overall reduction in aggregation propensity due to disruption of F/F hydrophobic collapse driven self-assembly by CH-π interactions. The glycosylation leads to increase in overall hydration of these peptides which is reflected in the changes in material properties such reduced formation of amyloid-like structures and enhanced thermostability. Therefore, we believe this to be a first step in understanding the changes in molecular interactions upon glycosylation and their implications in the design of self-assembling glycopeptide-based materials.

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