TY - JOUR
T1 - Adsorption of serum albumin onto octacalcium phosphate in supersaturated solutions regarding calcium phosphate phases
AU - Hamai, Ryo
AU - Tsuchiya, Kaori
AU - Suzuki, Osamu
N1 - Funding Information:
We thank Takamichi Miyazaki (Instrumental Analysis Group, Graduate School of Engineering, Tohoku University) for technical support for the TEM observations. This study was supported in part by MEXT/JSPS KAKENHI Grant Number JP17K19740 and JP18H02981.
Funding Information:
Funding: This study was supported in part by MEXT/JSPS KAKENHI Grant Number JP17K19740 and JP18H02981.
Publisher Copyright:
© 2019 by the authors.
PY - 2019/7/1
Y1 - 2019/7/1
N2 - Octacalcium phosphate (OCP) has been shown to enhance new bone formation, coupled with its own biodegradation, through osteoblasts and osteoclast-like cell activities concomitant with de novo hydroxyapatite (HA) formation and serum protein accumulation on its surface. However, the nature of the chemical environment surrounding OCP and how it affects its metabolism and regulates protein accumulation is unknown. The present study examined how the degree of supersaturation (DS) affects the bovine serum albumin (BSA) adsorption onto OCP in 150 mM Tris-HCl buffer at 37 °C and pH 7.4, by changing the Ca2+ ion concentration. The amount of BSA adsorbed onto OCP increased as the DS increased. In addition, the amount of newly formed calcium phosphate, which could be OCP, was increased, not only by increases in DS, but also at lower equilibrium concentrations of BSA. The increased adsorption capacity of BSA was likely related to the formation of calcium phosphate on the adsorbed OCP. Together the results suggested that the formation of new calcium phosphate crystals is dependent on both the DS value and the adsorbate protein concentration, which may control serum protein accumulation on the OCP surface in vivo.
AB - Octacalcium phosphate (OCP) has been shown to enhance new bone formation, coupled with its own biodegradation, through osteoblasts and osteoclast-like cell activities concomitant with de novo hydroxyapatite (HA) formation and serum protein accumulation on its surface. However, the nature of the chemical environment surrounding OCP and how it affects its metabolism and regulates protein accumulation is unknown. The present study examined how the degree of supersaturation (DS) affects the bovine serum albumin (BSA) adsorption onto OCP in 150 mM Tris-HCl buffer at 37 °C and pH 7.4, by changing the Ca2+ ion concentration. The amount of BSA adsorbed onto OCP increased as the DS increased. In addition, the amount of newly formed calcium phosphate, which could be OCP, was increased, not only by increases in DS, but also at lower equilibrium concentrations of BSA. The increased adsorption capacity of BSA was likely related to the formation of calcium phosphate on the adsorbed OCP. Together the results suggested that the formation of new calcium phosphate crystals is dependent on both the DS value and the adsorbate protein concentration, which may control serum protein accumulation on the OCP surface in vivo.
KW - Bovine serum albumin
KW - Degree of supersaturation
KW - Octacalcium phosphate
KW - Protein adsorption
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U2 - 10.3390/ma12142333
DO - 10.3390/ma12142333
M3 - Article
AN - SCOPUS:85070475292
VL - 12
JO - Materials
JF - Materials
SN - 1996-1944
IS - 14
M1 - 2333
ER -