A review of the aggregation properties of a recombinant amelogenin. Academic Article

abstract

• The present paper reviews some recent data on the aggregation properties of a recombinant amelogenin using dynamic light scattering, transmission electron microscopy, atomic force microscopy, and size exclusion chromatography. It was found that the recombinant amelogenin M179 molecules in solution form spherical monodisperse aggregates (15-20 nm) which are predominantly stabilized by intermolecular hydrophobic interactions while their surfaces are charged, carrying the hydrophilic carboxy-terminal sequence. We concluded that the spherical aggregates represent the "stippled materials" secreted by the ameloblasts at the mineralization front. We further speculate that the self-assembly process in the formation of amelogenin aggregates may play a primary role in the structural organization of mineralizing enamel.

published proceedings

• Connect Tissue Res

author list (cited authors)

• Moradian-Oldak, J., Simmer, J. P., Lau, E. C., Diekwisch, T., Slavkin, H. C., & Fincham, A. G.

citation count

• 36

complete list of authors

• Moradian-Oldak, J||Simmer, JP||Lau, EC||Diekwisch, T||Slavkin, HC||Fincham, AG

publication date

• January 1995

publisher

• Taylor & Francis  Publisher

published in

• Connective Tissue Research  Journal

keywords

• Agglutination
• Ameloblasts
• Amelogenin
• Animals
• Carbon Dioxide
• Chemical Phenomena
• Chemistry, Physical
• Chromatography
• Dental Enamel Proteins
• Light
• Mice
• Microscopy, Atomic Force
• Microscopy, Electron
• Recombinant Proteins
• Scattering, Radiation
• Structure-Activity Relationship

Digital Object Identifier (DOI)

• 10.3109/03008209509013714

start page

• 125

end page

• 130

volume

• 32

issue

• 1-4

URL

• http://dx.doi.org/10.3109/03008209509013714