Interaction of Taxol with intravenous immunoglobulin: An inhibition of Taxol from crystallizing in aqueous solution

Transmission Electron Microscopy of Pharmaceutical Materials

“…Its application to pharmaceutical materials, however, has been very limited. Some examples include imaging crystals of the compounds dipyridamole14 and taxol,15 and defects in liquid crystals of fenoprofen,16 and an electron diffraction study on roxifiban,17 but the full potential of the technique has yet to be fully appreciated.…”

Interaction of curcumin with intravenous immunoglobulin: A fluorescence quenching and Fourier transformation infrared spectroscopy study

“…Studies on the efficacy of an IgG F(ab) 2 preparation against taxol-induced C activation revealed that at a therapeutically relevant dose level (10 mg ml À1 ), this Fcdepleted IgG caused significant suppression of taxolinduced SC5b-9 formation, but replacing IVIG with 10 mg ml À1 human serum albumin (HSA) caused no inhibition of taxol-induced rise of SC5b-9 (Lutz et al 1996). Also, it is reported that within a range of molar concentration ratio of taxol to IVIG, the interaction of IVIG with taxol can inhibit taxol from crystallizing in aqueous solution (Liu et al 2008). Studies revealed that IVIG may stimulate the production of IL-12, an antitumor and anti-angiogenic cytokine, enhanced NK cell activity (Shoenfeld et al 2001), and can decrease the level of matrix metalloproteinase-9 (MMP-9) expression in the U937 monocyte line with a decrease in the m-RNA level of MMP-9, a vital step in the invasion of metastatic cancer cells.…”

2-(2-Hydroxy-5-nitrobenzylidene)-1,3-indanedione versus Fluorescein Isothiocyanate in Interaction with Anti-hFABP Immunoglobulin G1: Fluorescence Quenching, Secondary Structure Alteration and Binding Sites Localization

“…Each light chain has two domains (V L and C L ) and each heavy chain has four domains (V H , C H 1, C H 2 and C H 3). Each domain contains two cysteine (Cys) residues that form the intra-domain disulfide bond, and at least one Trp residue [15]. The domains are held together by disulfide bonds and non-covalent forces.…”

“…Although substituted indane-1,3-dione derivatives have been used in the fields of medicine [10] and biology [11], literature data on their chemical and physical interactions with proteins is scarce [12,13], and no chemical and physical studies of their interaction with immunoglobulins, and their applicability as fluorescent labels were found. Moreover, very few studies deal with the theoretical characterization of the small ligand–immunoglobulin interaction [14,15]. …”