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Non‐covalent interaction of 2', 4', 5', 7'‐tetrabromo‐4, 5, 6, 7‐tetrachlorofluorescein with proteins and its application
Author(s) -
Gao HongWen,
Zhao JianFu,
Yang QiaoZhi,
Liu XiangHu,
Chen Ling,
Pan LuTing
Publication year - 2006
Publication title -
proteomics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.26
H-Index - 167
eISSN - 1615-9861
pISSN - 1615-9853
DOI - 10.1002/pmic.200500715
Subject(s) - chemistry , hydrogen bond , van der waals force , covalent bond , hydrophobic effect , amino acid , attraction , isothermal titration calorimetry , absorbance , organic chemistry , chromatography , molecule , biochemistry , linguistics , philosophy
The interactions of 2', 4', 5', 7'‐tetrabromo‐4, 5, 6, 7‐tetrachlorofluorescein (TBTCF) with BSA, ovalbumin (OVA) and poly‐L‐lysine (PLYS) at pH 3.70 have been investigated by combination of the spectral correction technique and the Langmuir isothermal adsorption. The active connection actions such as ion pairs, van der Waals' force, hydrogen bond, hydrophobic bond were proposed to explain the non‐covalent interaction between TBTCF and BSA, OVA and PLYS. Effects of the electrolyte and high temperature indicated that union of the active connections between TBTCF and BSA and OVA was too firm to be destroyed. The relationship between the binding number of TBTCF and variety fraction of the amino acid residues was analyzed. The binding number of TBTCF depended on the number of positively charged amino acid residues. The other amino acid residues surrounded and seized TBTCF by hydrogen bonds and hydrophobic bonds when the electrostatic attraction pulled TBTCF to link protein. In addition, a novel method named the absorbance ratio difference was established for determination of protein in trace level and was applied with much higher sensitivity than the ordinary method.