Showing papers by "Anne Imberty published in 2023"
TL;DR: In this paper , the cell-free expressed lectins can be directly coupled with BLI analysis, either in solution or immobilized on the sensor, to measure interaction with carbohydrate ligands without purification.
Abstract: Lectins are important biological tools for binding glycans, but recombinant protein expression poses challenges for some lectin classes, limiting the pace of discovery and characterization. To discover and engineer lectins with new functions, workflows amenable to rapid expression and subsequent characterization are needed. Here, we present bacterial cell-free protein synthesis as a means for efficient, small-scale expression of multivalent, disulfide bond-rich, rhamnose-binding lectins. Furthermore, we demonstrate that the cell-free expressed lectins can be directly coupled with BLI analysis, either in solution or immobilized on the sensor, to measure interaction with carbohydrate ligands without purification. This workflow enables determination of lectin substrate specificity and estimation of binding affinity. Overall, we believe that this method will enable high-throughput expression, screening, and characterization of new and engineered multivalent lectins for applications in synthetic glycobiology.
1 citations
TL;DR: In this paper , the authors reported the copolymerization of 2-methylene-1,3,6-trioxocane (MTC) as a cyclic ketene acetals with vinyl ether (VE) or maleimide (MI) derivatives.
1 citations
TL;DR: In this article , the symmetry and number of supramolecular interactions introduced on protein surfaces could direct the formation of unspecific interactions between proteins and induce various nanoscale assemblies, including coiling nanowires, nanotubes, and nanosheets.
Abstract: Precise protein assemblies not only constitute a series of living machineries but also provide an advanced class of biomaterials. Previously, we developed the inducing ligand strategy to generate various fixed protein assemblies, without the formation of noncovalent interactions between proteins. Here, we demonstrated that controlling the symmetry and number of supramolecular interactions introduced on protein surfaces could direct the formation of unspecific interactions between proteins and induce various nanoscale assemblies, including coiling nanowires, nanotubes, and nanosheets, without manipulation of the protein's native surfaces. More importantly, these nanoscale assemblies could spontaneously evolve into more ordered architectures, crystals. We further showed that the transformation from the introduced supramolecular interactions to the interactions formed between proteins was crucial for pathway selection and outcomes of evolution. These findings reveal a transformation mechanism of protein self-assembly that has not been exploited before and may provide an approach to generate complex and transformable biomacromolecular self-assemblies.
TL;DR: In this article , the authors provide a view on the current strategy with a focus on synthetic biology approaches yielding to novel specificity, but other novel architectures with novel application in biotechnology or therapy.
TL;DR: In this paper , an online solution called BiotechLec (https://www.unilectin.eu/biotechlec) is proposed in a new section of UniLectin, a platform dedicated to lectin molecular knowledge.
Abstract: For decades lectins have been used as probes in glycobiology and this usage has gradually spread to other domains of Life Science. Nowadays, researchers investigate glycan recognition with lectins in diverse biotechnology and clinical applications addressing key questions regarding binding specificity. The latter is documented in scattered and heterogeneous sources and this situation begs for a centralized and easy-access reference. To address this need, an on-line solution called BiotechLec (https: //www.unilectin.eu/biotechlec) is proposed in a new section of UniLectin, a platform dedicated to lectin molecular knowledge.