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Interaction between Gold Nanoparticles and Bovine Serum Albumin or Sheep Antirabbit Immunoglobulin G
Author(s) -
Ao LiMei,
Gao Feng,
Pan BiFeng,
Cui DaXiang,
Gu HongChen
Publication year - 2006
Publication title -
chinese journal of chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.28
H-Index - 41
eISSN - 1614-7065
pISSN - 1001-604X
DOI - 10.1002/cjoc.200690048
Subject(s) - chemistry , colloidal gold , zeta potential , bovine serum albumin , tryptophan , nanoparticle , aqueous solution , quenching (fluorescence) , residue (chemistry) , nuclear chemistry , fluorescence , chromatography , biochemistry , nanotechnology , organic chemistry , amino acid , materials science , physics , quantum mechanics
Abstract The interaction between gold nanoparticles and proteins such as bovine serum albumin and immunoglobulin G under the condition of different pH values was studied based on the measurement of zeta potential and fluorescence quenching of the proteins before and after proteins were bound with gold nanoparticles. Aggregations were found in gold colloid aqueous solution after addition of proteins by TEM characterization and UV‐Vis spectroscopy determination. The results showed that the values of zeta potential were quite different, the binding constant K b and stoichiometry n were slightly increased with the increase of pH value. In conclusion, two factors could affect markedly the interaction between gold nanoparticles and proteins, that is, surface charge and the coordination effect between gold nanoparticles and indole group of the tryptophan residue of proteins.