Not all carboxylates are created equal: Differences in interaction of carboxylated peptides with a CaCO3 dimer

作者：Rosas Garcia Victor M^*; de Leon Abarte Isidro; Vidal Lopez German; Palacios Pargas Arturo; Jauregui Prado Xochitl

来源：Biophysical Chemistry, 2014, 192: 27-32.

DOI：10.1016/j.bpc.2014.06.003

• Asprich protein
• Aggregation
• Blind docking
• Crystallization
• Organic-inorganic interface

The carboxylate group has been considered the "glue" for mineralizing proteins because of its ability to bind Ca(II). We propose the calcium salts of dicarboxylated dipeptides (Asp-Asp and Glu-Glu) as the smallest models of a mineralizing protein active site. Molecular dynamics/simulated annealing was used for conformational search of the dipeptide global minimum. Semiempirical blind docking was used for configurational search of all cluster-peptide complexes and structures were then optimized in the gas phase at the RI-MP2/SVP level of theory. Solvent effects were also taken into account. We found that the energy of interaction of the calcium carboxylates with a calcium carbonate dimer can be either favorable or unfavorable depending on side-chain length, so side-chain carboxylic groups belonging to different amino acids may show different affinities towards calcium carbonate.

• 出版日期2014-8