Publications by authors named "E J Petersson"

Molecular rotor-based fluorophores (RBFs) that are target-selective and sensitive to both polarity and viscosity are valuable for diverse biological applications. Here, we have designed next-generation RBFs based on the underexplored bimane fluorophore through either changing in aryl substitution or varying π-linkages between the rotatable electron donors and acceptors to produce red-shifted fluorescence emissions with large Stokes shifts. RBFs exhibit a twisted intramolecular charge transfer mechanism that enables control of polarity and viscosity sensitivity, as well as target selectivity.

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Rare earth elements (REEs) are critical materials to modern technologies. They are obtained by selective separation from mining feedstocks consisting of mixtures of their trivalent cation. We are developing an all-aqueous, bioinspired, interfacial separation using peptides as amphiphilic molecular extractants.

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Article Synopsis
  • - The synthesis of crystallizable unnatural amino acid acridon-2-ylalanine (Acd) is refined for large-scale production, allowing its incorporation into proteins through genetic code expansion (GCE) and preparation for solid-phase peptide synthesis (SPPS).
  • - Acd is utilized in designing fluorescent protease sensors by leveraging its ability to quench fluorescence when near tyrosine (Tyr) residues, showcasing its application in biochemistry.
  • - The study also explores Acd's role in a lanthanide-binding peptide and its insertion into the protein α-synuclein, revealing its effectiveness in studying ion binding and aggregation properties in proteins.
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Large B-cell lymphomas (LBLs) comprise a genetically heterogeneous group of clinically aggressive non-Hodgkin lymphomas, frequently exhibiting overlapping features with diffuse large B-cell lymphoma and Burkitt's lymphoma. We report a case of a 24-year-old, previously healthy male with a classical clinical presentation of acute appendicitis. The pathologic examination discovered a large B-cell lymphoma with MYC and BCL6 rearrangements in the excised appendix.

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Dipeptidyl peptidase 4 (DPP-4) is a promising biomarker for cancer and metabolic diseases. We demonstrate the design of novel fluorescent DPP-4 probes based on the protease's native substrates using a thioamide as a quencher for measuring kinetics, inhibition with sitagliptin, and DPP-4 activity in saliva samples.

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