Hyunjun Yang

Mar 30, 2024 | pubs.rsc.org | Hailey Wallace |Hyunjun Yang |Sophia Tan

De novo design of peptides that bind specific conformers of α-synuclein† Insoluble amyloids rich in cross-β fibrils are observed in a number of neurodegenerative diseases. Depending on the clinicopathology, the amyloids can adopt distinct supramolecular assemblies, termed conformational strains. However, rapid methods to study amyloids in a conformationally specific manner are lacking.

Nov 16, 2023 | biorxiv.org | Hailey Wallace |Hyunjun Yang |Sophia Tan |Henry Pan

AbstractInsoluble amyloids rich in cross-beta fibrils are observed in a number of neurodegenerative diseases. Depending on the clinicopathology, the amyloids can adopt distinct supramolecular assemblies, termed conformational strains. However, rapid methods to study amyloid in a conformationally specific manner are lacking. We introduce a novel computational method for de novo design of peptides that tile the surface of alpha-synuclein fibrils in a conformationally specific manner.

Nov 13, 2023 | dx.doi.org | Hyunjun Yang |Adam G Kreutzer |James S Nowick |K. Ashley

Download Hi-Res ImageDownload to MS-PowerPointCite This:J. Org. Chem. 2024, XXXX, XXXRETURN TO ARTICLES ASAPPREVNoteNEXTHyunjun YangDepartment of Chemistry, University of California Irvine, Irvine, California 92697, United States, , and *James S. NowickDepartment of Chemistry, University of California Irvine, Irvine, California 92697, United StatesDepartment of Pharmaceutical Sciences, University of California Irvine, Irvine, California 92697, United States*Email: [email protected] this: J. Org.

Nov 13, 2023 | pubs.acs.org | Hyunjun Yang |Adam G Kreutzer |James S Nowick |K. Ashley

Download Hi-Res ImageDownload to MS-PowerPointCite This:J. Org. Chem. 2024, XXXX, XXXHyunjun YangDepartment of Chemistry, University of California Irvine, Irvine, California 92697, United States, , and *James S. NowickDepartment of Chemistry, University of California Irvine, Irvine, California 92697, United StatesDepartment of Pharmaceutical Sciences, University of California Irvine, Irvine, California 92697, United States*Email: [email protected] this: J. Org. Chem. 2024, XXXX, XXX.

Nov 1, 2023 | biorxiv.org | Hyunjun Yang |Adam G Kreutzer |James S Nowick

AbstractTeixobactin is a potent peptide antibiotic against Gram-positive bacteria that binds to lipid II and related peptidoglycan precursors and disrupts the cell membrane. This paper presents the X-ray crystallographic structure of the N-methylated teixobactin analogue N-Me-D-Gln4,Lys10-teixobactin (1). N-Methylation at position 4 prevents uncontrolled aggregation and enables the crystallization of the teixobactin analogue.