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STa peptide analogs for probing guanylyl cyclase C.
- Source :
-
Biopolymers [Biopolymers] 2008; Vol. 90 (5), pp. 713-23. - Publication Year :
- 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.
- Subjects :
- Amino Acid Sequence
Animals
Bacterial Toxins chemical synthesis
Bacterial Toxins genetics
Cell Line, Tumor
Cells, Cultured
Colorectal Neoplasms diagnosis
Colorectal Neoplasms enzymology
Colorectal Neoplasms microbiology
Disulfides metabolism
Drug Delivery Systems
Enterotoxins chemical synthesis
Enterotoxins genetics
Escherichia coli Infections diagnosis
Escherichia coli Infections enzymology
Escherichia coli Proteins
Guanylate Cyclase chemical synthesis
Humans
Intestinal Mucosa enzymology
Intestinal Mucosa microbiology
Mice
Molecular Sequence Data
Peptides administration & dosage
Peptides chemical synthesis
Peptides genetics
Receptors, Enterotoxin
Receptors, Guanylate Cyclase-Coupled
Bacterial Toxins metabolism
Enterotoxins metabolism
Guanylate Cyclase metabolism
Peptides metabolism
Receptors, Peptide metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 0006-3525
- Volume :
- 90
- Issue :
- 5
- Database :
- MEDLINE
- Journal :
- Biopolymers
- Publication Type :
- Academic Journal
- Accession number :
- 18615494
- Full Text :
- https://doi.org/10.1002/bip.21045