TY - JOUR
T1 - Effect of Biomolecules on the Nanostructure and Nanomechanical Property of Calcium-Silicate-Hydrate
AU - Kamali, Mahsa
AU - Ghahremaninezhad, Ali
N1 - Funding Information:
This study was partially supported by the NASA Florida Space Research Grant and University of Miami’s Provost Research Award.
PY - 2018/12/1
Y1 - 2018/12/1
N2 - Inspired by nature, this paper investigates the effect of biomolecules, such as amino acids and proteins, on the nanostructure and mechanical stiffness of calcium-silicate-hydrate (C-S-H). Amino acids with distinct functional groups, and proteins with different structures and compositions were used in the synthesis of the C-S-H nanocomposite. The atomic structure was examined using X-ray diffraction (XRD) and Fourier transform infrared spectroscopy (FTIR). The morphology was investigated using scanning electron microscopy (SEM) and atomic force microscopy (AFM). AFM nanoindentation was used to evaluate the Young's modulus of the modified C-S-H. Positively charged, H-bond forming and hydrophobic amino acids were shown to influence the atomic structure of C-S-H. The effect of negatively charged amino acid on atomic structure was more pronounced at higher C/S ratio. A noticeable increase in silicate polymerization of C-S-H modified with proteins at high C/S ratio was observed. The microscopic examination demonstrated a globular morphology for all samples except for C-S-H modified with hemoglobin, which showed a platelet morphology. The Young's modulus of C-S-H with amino acids and proteins showed a general reduction compared to that of the control C-S-H.
AB - Inspired by nature, this paper investigates the effect of biomolecules, such as amino acids and proteins, on the nanostructure and mechanical stiffness of calcium-silicate-hydrate (C-S-H). Amino acids with distinct functional groups, and proteins with different structures and compositions were used in the synthesis of the C-S-H nanocomposite. The atomic structure was examined using X-ray diffraction (XRD) and Fourier transform infrared spectroscopy (FTIR). The morphology was investigated using scanning electron microscopy (SEM) and atomic force microscopy (AFM). AFM nanoindentation was used to evaluate the Young's modulus of the modified C-S-H. Positively charged, H-bond forming and hydrophobic amino acids were shown to influence the atomic structure of C-S-H. The effect of negatively charged amino acid on atomic structure was more pronounced at higher C/S ratio. A noticeable increase in silicate polymerization of C-S-H modified with proteins at high C/S ratio was observed. The microscopic examination demonstrated a globular morphology for all samples except for C-S-H modified with hemoglobin, which showed a platelet morphology. The Young's modulus of C-S-H with amino acids and proteins showed a general reduction compared to that of the control C-S-H.
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U2 - 10.1038/s41598-018-27746-x
DO - 10.1038/s41598-018-27746-x
M3 - Article
C2 - 29934541
AN - SCOPUS:85048937955
VL - 8
JO - Scientific Reports
JF - Scientific Reports
SN - 2045-2322
IS - 1
M1 - 9491
ER -