Three-step one-pot methodology for functionalization of sterically hindered polyacrylates

A new publication from the group in Polymer Chemistry addresses the functionalization of sterically hindered polyacrylates. Unlike poly(methyl acrylate) (PMA), the chain ends of which can be reacted quantitatively after polymerization, the chain ends of poly(butyl acrylate) (PBA) show lower reactivity due to steric encumbrance. In this work, a three step methodology involving biphasic SET-LRP, chain extension with methyl acrylate and heterogeneous esterification provides a route to acrylate-functionalized PBA. This approach, which can be simplified by applying two or even all three steps in a single pot, may provide a more general route to the funcationalization of sterically hindered polyacrylates.

This work was led in the group by Adrian Moreno with contributions from Tong Liu, as part of a collaboration with the group of Gerard Lligadas at University Rovira i Virgili, Tarragona, Spain.

SET-LRP Applied to Hydrophobic Biobased Menthyl Acrylate

Recent collaborative work from the group broadening the scope of SET-LRP has been published in Biomacromolecules. The new paper details the polymerization of menthyl acrylate, a monomer derived from biobased and renewable menthol. This monomer’s hydrophobicity, which might be expected to be problematic for SET-LRP, instead causes the reaction to self-generate a biphasic system, in which SET-LRP proceeds cleanly.

This work was led by the group of Gerard Lligadas at University Rovira i Virgili, Tarragona, Spain.

SET-LRP’s High Chain End Functionality Exploited to Create Complex Architecture

Recent work published by the group in Polymer Chemistry utilizes one of the key features of single-electron transfer-living radical polymerization (SET-LRP): the high chain end functionality of the resulting polymers. In this work, led in our group by Adrian Moreno with contributions from Ryan L. Jezorek and Tong Liu, functional end groups of poly(methyl acrylate) (PMA) are exploited for esterification to generate PMA macromonomers and telechelics.

This work was conducted as part of a collaboration with the group of Gerard Lligadas at University Rovira i Virgili, Tarragona, Spain.

Latest Paper in PNAS Unravels the Complexity of Lectin-Carbohydrate Interactions

The group has published a new paper in Proceedings of the National Academy of Sciences. The work presents a platform for interrogating the binding interactions between lectins and carbohydrates via agglutination assays. This approach is applied to understand the complex interplay between lectin structure, glycodendrimersome surface charge, glycan density, and cross-linking.

The work was led in our group by Qi Xiao with contributions from Irene Buzzacchera and Samuel E. Sherman, as part of a multidisciplinary collaborative effort with the groups of Hans-Joachim Gabius (Ludwig-Maximilians-University, Munich, Germany), Daniel A. Hammer (Penn), Michael L. Klein (Temple University, Philadelphia) and Martin Möller (RWTH Aachen University, Aachen, Germany).

New Work Uses Cheaper TREN as Ligand for SET-LRP

The group has published a new paper in Polymer Chemistry. The work examines the replacement of Me6-TREN, a common ligand for SET-LRP, by TREN, which is 80 times cheaper. It is shown that high chain end functionality and controlled polymer growth can be achieved in a diverse range of water-organic solvent mixtures, further reducing the cost of SET-LRP for large-scale application.

The work was led in our group by Adrian Moreno and Silvia Grama, as part of a collaboration with the group of Gerard Lligadas at University Rovira i Virgili, Tarragona, Spain.

New Paper in Angewandte Chemie Designated as a Hot Paper

A paper recently published by the group in Angewandte Chemie International Edition has been designated as a Hot Paper. The paper reports the use of glycodendrimersomes as a platform for the interrogation of sugar binding to a variety of natural and engineered human lectins, to examine the impact of spatial factors on aggregation activity. It was discovered that two aspects of lectin functionality respond non-uniformly to structural changes in the lectins.

The work was led in our group by Qi Xiao in collaboration with researchers from Ruprecht-Karls-University Heidelberg (Germany), Ludwig-Maximilians-University Munich (Germany), CSIC Ramiro de Maeztu (Spain), and Temple University (Philadelphia, PA).