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Title: Interactions of amelogenin with phospholipids

Journal Article · · Biopolymers
DOI:https://doi.org/10.1002/bip.22573· OSTI ID:1342890
 [1];  [1];  [2];  [2];  [2];  [1]
  1. Univ. of Southern California, Los Angeles, CA (United States)
  2. New York Univ., New York, NY (United States)

Amelogenin protein has the potential to interact with other enamel matrix proteins, mineral, and cell surfaces. In this paper, we investigated the interactions of recombinant amelogenin rP172 with small unilamellar vesicles as model membranes, toward the goal of understanding the mechanisms of amelogenin–cell interactions during amelogenesis. Dynamic light scattering (DLS), fluorescence spectroscopy, circular dichroism (CD), and nuclear magnetic resonance (NMR) were used. In the presence of phospholipid vesicles, a blue shift in the Trp fluorescence emission maxima of rP172 was observed (~334 nm) and the Trp residues of rP172 were inaccessible to the aqueous quencher acrylamide. DLS studies indicated complexation of rP172 and phospholipids, although the possibility of fusion of phospholipids following amelogenin addition cannot be ruled out. NMR and CD studies revealed a disorder–order transition of rP172 in a model membrane environment. Strong fluorescence resonance energy transfer from Trp in rP172 to DNS-bound-phospholipid was observed, and fluorescence polarization studies indicated that rP172 interacted with the hydrophobic core region of model membranes. Finally, our data suggest that amelogenin has ability to interact with phospholipids and that such interactions may play key roles in enamel biomineralization as well as reported amelogenin signaling activities.

Research Organization:
New York Univ. (NYU), NY (United States)
Sponsoring Organization:
USDOE Office of Science (SC), Basic Energy Sciences (BES)
Grant/Contract Number:
FG02-03ER46099
OSTI ID:
1342890
Journal Information:
Biopolymers, Vol. 103, Issue 2; ISSN 0006-3525
Publisher:
WileyCopyright Statement
Country of Publication:
United States
Language:
English
Citation Metrics:
Cited by: 10 works
Citation information provided by
Web of Science

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Cited By (2)

TGF-β1 autocrine signalling and enamel matrix components journal September 2016
Molecular insights into hypomineralized enamel journal April 2019