TY - JOUR

T1 - Three Reasons Why Aspartic Acid and Glutamic Acid Sequences Have a Surprisingly Different Influence on Mineralization

AU - Lemke, Tobias

AU - Edte, Moritz

AU - Gebauer, Denis

AU - Peter, Christine

N1 - Funding Information: We thank Christoph Globisch and Nicolas Schneider for proofreading and for very helpful feedback. We thank Maxim Gindele for valuable discussions regarding the experimental background. We gratefully acknowledge funding by the German Research Foundation (DFG) through SFB1214. The authors acknowledge support by the state of Baden-Württemberg through bwHPC and the DFG through grant INST 37/935-1 FUGG.

PY - 2021/9/16

Y1 - 2021/9/16

N2 - Understanding the role of polymers rich in aspartic acid (Asp) and glutamic acid (Glu) is the key to gaining precise control over mineralization processes. Despite their chemical similarity, experiments revealed a surprisingly different influence of Asp and Glu sequences. We conducted molecular dynamics simulations of Asp and Glu peptides in the presence of calcium and chloride ions to elucidate the underlying phenomena. In line with experimental differences, in our simulations, we indeed find strong differences in the way the peptides interact with ions in solution. The investigated Asp pentapeptide tends to pull a lot of ions into its vicinity, and many structures with clusters of calcium and chloride ions on the surface of the peptide can be observed. Under the same conditions, comparatively fewer ions can be found in proximity of the investigated Glu pentapeptide, and the structures are characterized by single calcium ions bound to multiple carboxylate groups. Based on our simulation data, we identified three reasons contributing to these differences, leading to a new level of understanding additive-ion interactions.

AB - Understanding the role of polymers rich in aspartic acid (Asp) and glutamic acid (Glu) is the key to gaining precise control over mineralization processes. Despite their chemical similarity, experiments revealed a surprisingly different influence of Asp and Glu sequences. We conducted molecular dynamics simulations of Asp and Glu peptides in the presence of calcium and chloride ions to elucidate the underlying phenomena. In line with experimental differences, in our simulations, we indeed find strong differences in the way the peptides interact with ions in solution. The investigated Asp pentapeptide tends to pull a lot of ions into its vicinity, and many structures with clusters of calcium and chloride ions on the surface of the peptide can be observed. Under the same conditions, comparatively fewer ions can be found in proximity of the investigated Glu pentapeptide, and the structures are characterized by single calcium ions bound to multiple carboxylate groups. Based on our simulation data, we identified three reasons contributing to these differences, leading to a new level of understanding additive-ion interactions.

UR - http://www.scopus.com/inward/record.url?scp=85114893239&partnerID=8YFLogxK

U2 - 10.1021/acs.jpcb.1c04467

DO - 10.1021/acs.jpcb.1c04467

M3 - Article

VL - 125

SP - 10335

EP - 10343

JO - The Journal of Physical Chemistry B

JF - The Journal of Physical Chemistry B

SN - 1520-6106

IS - 36

ER -