J
James W. Checco
Researcher at University of Nebraska–Lincoln
Publications - 26
Citations - 573
James W. Checco is an academic researcher from University of Nebraska–Lincoln. The author has contributed to research in topics: Peptide & Medicine. The author has an hindex of 8, co-authored 17 publications receiving 425 citations. Previous affiliations of James W. Checco include University of Illinois at Urbana–Champaign & University of Wisconsin-Madison.
Papers
More filters
Journal ArticleDOI
α/β-Peptide Foldamers Targeting Intracellular Protein–Protein Interactions with Activity in Living Cells
James W. Checco,Erinna F. Lee,Erinna F. Lee,Marco Evangelista,Nerida J. Sleebs,Kelly L. Rogers,Kelly L. Rogers,Anne Pettikiriarachchi,Nadia J. Kershaw,Nadia J. Kershaw,Geoffrey A. Eddinger,David G. Belair,Julia L. Wilson,Chelcie H. Eller,Ronald T. Raines,William L. Murphy,Brian J. Smith,Samuel H. Gellman,W. Douglas Fairlie,W. Douglas Fairlie +19 more
TL;DR: The results show that backbone modification, a strategy that has received relatively little attention in terms of peptide engineering for biomedical applications, can be combined with more commonly deployed peripheral modifications such as side chain cross-linking to produce synergistic benefits.
Journal ArticleDOI
Targeting diverse protein–protein interaction interfaces with α/β-peptides derived from the Z-domain scaffold
James W. Checco,Dale F. Kreitler,Nicole C. Thomas,David G. Belair,Nicholas J. Rettko,William L. Murphy,Katrina T. Forest,Samuel H. Gellman +7 more
TL;DR: A strategy for designing oligomers containing both α- and β-amino acid residues (“α/β-peptides”) that mimic several peptides derived from the three-helix bundle “Z-domain” scaffold that should enable the design of biostable α/ β- peptides that bind tightly and specifically to diverse targets of biomedical interest.
Journal ArticleDOI
Extending Foldamer Design beyond α-Helix Mimicry: α/β-Peptide Inhibitors of Vascular Endothelial Growth Factor Signaling
Holly S. Haase,Kimberly J. Peterson-Kaufman,Sheeny K. Lan Levengood,James W. Checco,William L. Murphy,Samuel H. Gellman +5 more
TL;DR: Efforts to develop peptidic foldamers that bind to the irregular receptor-recognition surface of vascular endothelial growth factor (VEGF) are described and homologues that contain up to ~30% β residues, retain significant affinity for VEGF, and display substantial resistance to proteolysis are identified.
Journal ArticleDOI
Targeting recognition surfaces on natural proteins with peptidic foldamers
TL;DR: Important recent advances in this area have involved enhancing membrane permeability to provide access to intracellular protein targets, improving pharmacokinetics and duration of action in vivo, and developing strategies appropriate for targeting large and irregularly-shaped protein surfaces.
Journal ArticleDOI
Structure-guided rational design of α/β-peptide foldamers with high affinity for BCL-2 family prosurvival proteins.
Brian J. Smith,Erinna F. Lee,Erinna F. Lee,James W. Checco,Marco Evangelista,Samuel H. Gellman,W. Douglas Fairlie,W. Douglas Fairlie +7 more
TL;DR: The findings demonstrate that structure‐guided rational design can be used to improve affinity and alter partner selectivity of peptidic ligands with unnatural backbones that bind to specific protein partners.