TY - JOUR
T1 - Incorporation of fluorescent molecules and proteins into calcium oxalate monohydrate single crystals
AU - Touryan, Lara A.
AU - Clark, Ruti H.
AU - Gurney, Richard W.
AU - Stayton, Patrick S.
AU - Kahr, Bart
AU - Vogel, Viola
N1 - Funding Information:
The authors thank Dr. M.J. Lochhead (University of New Hampshire, Durham NH) for technical assistance and his many contributions to this project. Dr. Allison Campbell (Battelle Pacific Northwest National Laboratory) and NIH Dental Institute provided support and funding. LT acknowledges support from a University of Washington Center for Nanotechnology graduate award. BK acknowledges support from the NSF.
PY - 2001/11
Y1 - 2001/11
N2 - A central question to understanding biomineralization is determining how biomolecules are integrated within inorganic host lattices, thereby changing material properties yet retaining single crystal structure of the biomineral. We have addressed guest incorporation within single biomineral crystals by investigating face specificity, anisotropy and the role of charges in fluorescent calcium oxalate monohydrate (COM) crystals nucleated from solutions containing eosin Y, fluoresceins and rhodamines. Additionally, we have examined the specificity of incorporation of Protein G wild-type (G-wt) and its mutant (G-Δ6, in which four aspartic acids and two glutamic acids have been replaced by the corresponding asparagine or glutamine), where G-wt promotes and G-Δ6 inhibits COM crystal growth. We found that (1) the negatively charged fluorophores, as well as the fluorophore-labeled proteins, G-wt and G-Δ6, were successfully incorporated during growth into the same {110} growth sectors in preferenc e to all others; (2) the positively charged TRITC (tetramethyl rhodamine isothiocyanate) was not incorporated as free fluorophore, but it became incorporated if conjugated to G-wt and G-Δ6; (3) once the fluorophores are incorporated, the polarization measurements of adsorption and emission were similar irrespectively whether taken from COM containing the free fluorophores, or the protein conjugates. The anisotropy was similar for rhodamines and fluoresceins.
AB - A central question to understanding biomineralization is determining how biomolecules are integrated within inorganic host lattices, thereby changing material properties yet retaining single crystal structure of the biomineral. We have addressed guest incorporation within single biomineral crystals by investigating face specificity, anisotropy and the role of charges in fluorescent calcium oxalate monohydrate (COM) crystals nucleated from solutions containing eosin Y, fluoresceins and rhodamines. Additionally, we have examined the specificity of incorporation of Protein G wild-type (G-wt) and its mutant (G-Δ6, in which four aspartic acids and two glutamic acids have been replaced by the corresponding asparagine or glutamine), where G-wt promotes and G-Δ6 inhibits COM crystal growth. We found that (1) the negatively charged fluorophores, as well as the fluorophore-labeled proteins, G-wt and G-Δ6, were successfully incorporated during growth into the same {110} growth sectors in preferenc e to all others; (2) the positively charged TRITC (tetramethyl rhodamine isothiocyanate) was not incorporated as free fluorophore, but it became incorporated if conjugated to G-wt and G-Δ6; (3) once the fluorophores are incorporated, the polarization measurements of adsorption and emission were similar irrespectively whether taken from COM containing the free fluorophores, or the protein conjugates. The anisotropy was similar for rhodamines and fluoresceins.
KW - A1. Biocrystallization
KW - A1. Doping
KW - B1. Calcium compounds
KW - B1. Proteins
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U2 - 10.1016/S0022-0248(01)01441-5
DO - 10.1016/S0022-0248(01)01441-5
M3 - Article
AN - SCOPUS:0035502133
SN - 0022-0248
VL - 233
SP - 380
EP - 388
JO - Journal of Crystal Growth
JF - Journal of Crystal Growth
IS - 1-2
ER -