Ontology highlight
ABSTRACT:
SUBMITTER: Su J
PROVIDER: S-EPMC6410667 | biostudies-literature | 2019 Feb
REPOSITORIES: biostudies-literature
Su Jingtan J Kegulian Natalie C NC Arun Bapat Rucha R Moradian-Oldak Janet J
ACS omega 20190201 2
Ameloblastin (Ambn), the most abundant non-amelogenin enamel protein, is intrinsically disordered and has the potential to interact with other enamel proteins and with cell membranes. Here, through multiple biophysical methods, we investigated the interactions between Ambn and large unilamellar vesicles (LUVs), whose lipid compositions mimicked cell membranes involved in epithelial cell-extracellular matrix adhesion. Using a series of Ambn Trp/Phe variants and Ambn mutants, we further showed tha ...[more]