Enamel protein chemistry--past, present and future

Area of Science:

• Biochemistry
• Dental Research
• Materials Science

Background:

• Enamel protein chemistry is complex, with young enamel containing ~20 distinct components.
• These components exist in dynamic equilibrium with larger aggregates.
• Significant changes occur during enamel maturation, involving selective protein removal.

Purpose of the Study:

• To review past progress in enamel protein chemistry.
• To assess the current state of knowledge on enamel protein composition and dynamics.
• To identify key challenges and unsolved problems in the field.

Main Methods:

• Literature review of existing research on enamel protein chemistry.
• Analysis of the composition and molecular weights of enamel protein components.
• Discussion of potential mechanisms for mineralization and protein removal.

Main Results:

• Young enamel matrix is a complex system of ~20 components (3-16 kDa).
• Maturation involves selective removal of most components, with amelogenins (proline/histidine-rich) removed first.
• 'Tuft protein' (serine/glycine-rich) is often retained in mature enamel.
• Some components isolated; partial sequences known for phosphoserine-containing proteins.

Conclusions:

• Significant advancements have been made in characterizing enamel proteins.
• The precise mechanisms of mineralization and protein removal remain unknown.
• The fundamental nature of the overall enamel protein system is the primary unsolved problem.