STa peptide analogs for probing guanylyl cyclase C.
Publication/Presentation Date
1-1-2008
Abstract
Guanylyl cyclase C (GC-C), universally overexpressed on primary and metastatic colorectal carcinoma cells, is activated by endogenous ligands, guanylin, and uroguanylin, and by exogenous 18-residue heat-stable enterotoxins (STa) produced by diarrheagenic bacteria. Two 12-residue STa analogs with alternate combinations of two interlocked disulfide bonds, peptides 3 and 6, were synthesized by orthogonal solid phase synthesis routes. Peptides 3 and 6 bound GC-C with a rank order potency of STa > peptide 3 > peptide 6. Peptides 3 and 6 behaved as agonists in stimulating cGMP production. The results reveal that the toxic domain of STa can be reduced to 12 amino acids.
Volume
90
Issue
5
First Page
713
Last Page
723
ISSN
0006-3525
Published In/Presented At
Tian, X., Michal, A. M., Li, P., Wolfe, H. R., Waldman, S. A., & Wickstrom, E. (2008). STa peptide analogs for probing guanylyl cyclase C. Biopolymers, 90(5), 713–723. https://doi.org/10.1002/bip.21045
Disciplines
Business Administration, Management, and Operations | Health and Medical Administration | Management Sciences and Quantitative Methods
PubMedID
18615494
Department(s)
Administration and Leadership
Document Type
Article