Arylamide derivatives as peptidomimetic inhibitors of calmodulin. Academic Article

abstract

• [structure: see text] Many peptides bind to calmodulin (CaM) in a helical conformation. Here we describe a group of synthetic inhibitors of CaM based on an arylamide scaffold that is intended to mimic smMLCK, a CaM-binding helical peptide. Compound 1 showed a K(i) value of 7.10 +/- 1.48 nM in a fluorescence polarization assay that monitors the strong association of CaM and its peptide ligand mastoparan X. ((1)H,(15)N)-HSQC NMR spectroscopy experiments suggested that 1 binds to CaM in an analogous fashion to that of smMLCK.

authors

• Wand, Joshua

published proceedings

• Org Lett

author list (cited authors)

• Yin, H., Frederick, K. K., Liu, D., Wand, A. J., & Degrado, W. F.

citation count

• 34

complete list of authors

• Yin, Hang||Frederick, Kendra K||Liu, Dahui||Wand, A Joshua||Degrado, William F

publication date

• January 2006

publisher

• American Chemical Society (ACS)  Publisher

published in

• Organic Letters  Journal

keywords

• Amides
• Amino Acid Sequence
• Calmodulin
• Fluorescence Polarization
• Molecular Structure
• Nuclear Magnetic Resonance, Biomolecular
• Peptides
• Protein Conformation

PubMed Central ID

• 16408880

Digital Object Identifier (DOI)

• 10.1021/ol052478j

start page

• 223

end page

• 225

volume

• 8

issue

• 2

URL

• http://dx.doi.org/10.1021/ol052478j