A review of the aggregation properties of a recombinant amelogenin.
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.
Moradian-Oldak
J
J
Center for Craniofacial Molecular Biology, School of Dentistry, University of Southern California, Los Angeles 90033, USA.
Simmer
J P
JP
Lau
E C
EC
Diekwisch
T
T
Slavkin
H C
HC
Fincham
A G
AG
D000371:Agglutination; D000565:Ameloblasts / Q000378:metabolism; D053523:Amelogenin; D000818:Animals; D002245:Carbon Dioxide / Q000737:chemistry; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D002845:Chromatography; D003746:Dental Enamel Proteins / Q000737:chemistry* / Q000378:metabolism / Q000648:ultrastructure; D008027:Light; D051379:Mice; D018625:Microscopy, Atomic Force; D008854:Microscopy, Electron; D011994:Recombinant Proteins; D012542:Scattering, Radiation; D013329:Structure-Activity Relationship
D053523:Amelogenin; C507200:Amelx protein, mouse; D003746:Dental Enamel Proteins; D011994:Recombinant Proteins; D002245:Carbon Dioxide; C041069:carboxyl radical