ISSN:
1573-0875
Source:
Springer Online Journal Archives 1860-2000
Topics:
Biology
,
Geosciences
Notes:
Abstract Unlike glutamic acid, L-γ-carboxyglutamic acid does not oligomerize efficiently when treated with carbonyldiimidazole in aqueous solution. However, divalent ions such as Mg2+ catalyze the reaction, and lead to the formation of oligomers in good yield. In the presence of hydroxylapatite, L-γ-carboxyglutamic acid oligomerizes efficiently in a reaction that proceeds in the absence of divalent ions but is further catalyzed when they are present. After ‘feeding’ 50 times with activated amino acid in the presence of the Mg2+ ion, oligomers longer than the 20-mer could be detected. The effect of hydroxylapatite on peptide elongation is very sensitive to the nature of the activated amino acid and the acceptor peptide. Glutamic acid oligomerizes more efficiently than L-γ-carboxyglutamic acid on hydroxylapatite and adds more efficiently to decaglutamic acid in solution. One might, therefore, expect that glutamic acid would add more efficiently than L-γ-carboxyglutamic acid to decaglutamic acid on hydroxylapatite. The contrary is true – the addition of L- γ-carboxyglutamic acid is substantially more efficient. This suggests that oligomerization on the surface of hydroxylapatite depends on the detailed match between the structure of the surface of the mineral and the structure of the oligomer.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1023/A:1006512304332
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