439948-71-7Relevant academic research and scientific papers
Facially amphiphilic polymers and oligomers and uses thereof
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, (2016/02/12)
The present invention discloses methods of use of facially amphiphilic polymers and oligomers, including pharmaceutical uses of the polymers and oligomers as antimicrobial agents and antidotes for hemorrhagic complications associated with heparin therapy.
Arylamide derivatives as allosteric inhibitors of the integrin α2β1/type I collagen interaction
Yin, Hang,Gerlach, Lars Ole,Miller, Meredith W.,Moore, David T.,Liu, Dahui,Vilaire, Gaston,Bennett, Joel S.,DeGrado, William F.
, p. 3380 - 3382 (2007/10/03)
We herein report a group of allosteric inhibitors of integrin α2β1 based on an arylamide scaffold. Compound 4 showed an IC50 of 4.80 μM in disrupting integrin I-domain/collagen binding in an ELISA. These arylamide compound
Arylamide derivatives as peptidomimetic inhibitors of calmodulin
Yin, Hang,Frederick, Kendra K.,Liu, Dahui,Wand, A. Joshua,DeGrado, William F.
, p. 223 - 225 (2007/10/03)
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 Ki 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. (1H,15N)-HSQC NMR spectroscopy experiments suggested that 1 binds to CaM in an analogous fashion to that of smMLCK.
