University of Nebraska-Lincoln
409D Hamilton Hall
Lincoln, NE 68588-0304
Postdoctoral Fellow, University of Illinois at Urbana-Champaign
Ph.D., University of Wisconsin-Madison
B.A., St. Olaf College
Our work focuses on understanding neuropeptides and peptide hormones that act as cell-to-cell signaling molecules. These biomolecules are important because their functions underlie critical biological processes and complex behaviors. Mimicking or antagonizing peptide-receptor interactions are critical strategies for understanding normal cell-to-cell communication and for treating diseases caused by signal dysregulation. Despite their importance in biology, the molecular-level details governing the signaling of many peptides are not well-understood. To address this challenge, the Checco Lab develops strategies to identify previously uncharacterized peptide-protein interactions, and to design novel compounds to modulate these interactions in a desired manner. From this work, our research will advance the understanding of specific cell-cell signaling pathways, identify new pathways for further exploration, and provide innovative starting points for future therapeutics.
Some active areas of research in the group include:
- Identifying the receptors for specific neuropeptides and peptide hormones involved in disease.
- Organic synthesis of complex peptides containing non-natural functional groups for use as chemical probes.
- Mass spectrometry-based identification and quantification of the processed forms of neuropeptides and peptide hormones from biological samples.
Students and researchers in the Checco Lab gain expertise in a diverse set of synthetic, analytical, and biological techniques, including chemical peptide synthesis, mass spectrometry-based analysis of protein mixtures, cell culture, and cell-based signaling assays.
For more information, please visit the Checco Research Group Homepage.
(1) Checco JW, Zhang G, Yuan W, Le Z, Jing J, Sweedler JV. “Aplysia allatotropin-related peptide and its newly identified D-amino acid-containing peptide epimer both activate a receptor and a neuronal target.” J. Biol. Chem. (2018) 293, 16862-16873. DOI: 10.1074/jbc.RA118.004367
(2) Checco JW, Zhang G, Yuan W, Yu K, Yin S, Roberts-Galbraith RH, Yau PM, Romanova EV, Jing J, Sweedler JV. “Molecular and physiological characterization of a receptor for D-amino acid-containing neuropeptides.” ACS Chem. Biol. (2018) 13, 1343-1352. DOI: 10.1021/acschembio.8b00167
(3) Checco JW, Gellman SH. “Iterative non-proteinogenic residue incorporation yields α/β-peptides with a helix-loop-helix tertiary structure and high affinity for VEGF.” ChemBioChem. (2017) 18, 291-299. DOI: 10.1002/cbic.201600545
(4) Checco JW, Lee EF, Evangelista M, Sleebs N, Rogers K, Pettikiriarachchi A, Kershaw N, Eddinger GA, Wilson JL, Belair DG, Eller CH, Raines RT, Murphy WL, Smith BJ, Gellman SH, Fairlie WD. “α/β-Peptide foldamers targeting intracellular protein-protein interactions with activity in living cells.” J. Am. Chem. Soc. (2015) 137, 11365-11375. DOI: 10.1021/jacs.5b05896
(5) Checco JW, Kreitler DF, Thomas NC, Belair DG, Rettko NJ, Murphy WL, Forest KT, Gellman SH. “Targeting diverse protein-protein interaction interfaces with α/β-peptides derived from the Z-domain scaffold.” Proc. Natl. Acad. Sci. U.S.A. (2015) 112, 4552-4557. DOI: 10.1073/pnas.1420380112