Interactions of amelogenin with phospholipids

Sowmya Bekshe Lokappa, Karthik Balakrishna Chandrababu, Kaushik Dutta, Iva Perovic, John Evans, Janet Moradian-Oldak

Research output: Contribution to journalArticle

Abstract

Amelogenin protein has the potential to interact with other enamel matrix proteins, mineral, and cell surfaces. 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 (sim;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. 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.

Original languageEnglish (US)
Pages (from-to)96-108
Number of pages13
JournalBiopolymers - Peptide Science Section
Volume103
Issue number2
DOIs
StatePublished - Feb 1 2015

Fingerprint

Amelogenin
Phospholipids
Enamels
Dichroism
Dynamic light scattering
Membranes
Circular Dichroism
Fluorescence
Nuclear magnetic resonance
Proteins
Biomineralization
Amelogenesis
Magnetic Resonance Spectroscopy
Order disorder transitions
Fluorescence spectroscopy
Unilamellar Liposomes
Fluorescence Resonance Energy Transfer
Complexation
Fluorescence Polarization
Acrylamide

Keywords

  • amelogenin
  • cell membrane
  • enamel
  • intrinsically disordered protein
  • lipid vesicles

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Biomaterials
  • Organic Chemistry

Cite this

Bekshe Lokappa, S., Balakrishna Chandrababu, K., Dutta, K., Perovic, I., Evans, J., & Moradian-Oldak, J. (2015). Interactions of amelogenin with phospholipids. Biopolymers - Peptide Science Section, 103(2), 96-108. https://doi.org/10.1002/bip.22573

Interactions of amelogenin with phospholipids. / Bekshe Lokappa, Sowmya; Balakrishna Chandrababu, Karthik; Dutta, Kaushik; Perovic, Iva; Evans, John; Moradian-Oldak, Janet.

In: Biopolymers - Peptide Science Section, Vol. 103, No. 2, 01.02.2015, p. 96-108.

Research output: Contribution to journalArticle

Bekshe Lokappa, S, Balakrishna Chandrababu, K, Dutta, K, Perovic, I, Evans, J & Moradian-Oldak, J 2015, 'Interactions of amelogenin with phospholipids', Biopolymers - Peptide Science Section, vol. 103, no. 2, pp. 96-108. https://doi.org/10.1002/bip.22573
Bekshe Lokappa S, Balakrishna Chandrababu K, Dutta K, Perovic I, Evans J, Moradian-Oldak J. Interactions of amelogenin with phospholipids. Biopolymers - Peptide Science Section. 2015 Feb 1;103(2):96-108. https://doi.org/10.1002/bip.22573
Bekshe Lokappa, Sowmya ; Balakrishna Chandrababu, Karthik ; Dutta, Kaushik ; Perovic, Iva ; Evans, John ; Moradian-Oldak, Janet. / Interactions of amelogenin with phospholipids. In: Biopolymers - Peptide Science Section. 2015 ; Vol. 103, No. 2. pp. 96-108.
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