Human serum albumin (HSA) is the most abundant protein in the blood plasma. Drug binding to HSA is crucial to study the absorption, distribution, metabolism, efficiency and bioavailability of drug molecules. In this study, isothermal titration calorimetry and molecular dynamics simulation of HSA and its complex with indometacin (IM) were performed to investigate thermodynamics parameters and th...

background: the affinity of an antibody to its antigen is a crucial parameter in its biological activity and performance of an immunoassay such as elisa. affinity of most igg specific mabs are often determined by methods which require labeling of either antigen or antibody, and are sometimes difficult to control, do not always lead to the expected signal and often result in immunological modifi...

mechanism of the binding of lomefloxacin (lmf) with human serum albumin has been studied at physiological ph (7.4) using fluorescence spectroscopic technique. lmf is a third-generation fluoroquinolone antibiotic that exhibits striking potency against a broad spectrum of gram-negative and gram-positive bacteria through inhibition of dna gyrase. lomefloxacin is a drug that is excreted in urine an...

background: among diverse protein purification systems, affinity chromatography is the most attractive one in the purification process of coagulation factors. coagulation factor vii is a plasma serine protease that has a significant role in natural human hemostasis and its recombinant form such as aryoseventm, has been applied in clinical treatment of bleeding disorders. immunoaffinity chromato...

hepatitis c virus (hcv) encodes two envelope glycoproteins, e1 and e2. our previous work selected a specific aptamer ze2, which could bind to e2 with high affinity, with a great potential for developing new molecular probes as an early diagnostic reagents or therapeutic drugs targeting hcv. in this study, the binding sites between e2 and aptamer ze2 were further explored. e2 was truncated to 15...

Isotherms of the binding of the anthracycIine antibiotic, adriamycin (adriblastin), to DNA histone complexes was studied by means of spectroscopic analysis. The results indicated that: (a) binding of adriamycin to histones reduced the interaction of histones with DNA, (b) binding of the drug to DNA did not change the binding affinity of histone to DNA and, (c) in the explored binding range...

Objective(s): Nanobodies, the single domain antigen binding fragments of heavy chain-only antibodies occurring naturally in camelid sera, are the smallest intact antigen binding entities. Their minimal size assists in reaching otherwise largely inaccessible regions of antigens. However, their camelid origin raises a possible concern of immunogenicity when used for human therapy. Humanization is...

To obtain drugs which are more selective at benzodiazepine (BZD) receptors, design and synthesis of functionally selective ligands for BZD receptors is the current strategy of our pharmaceutical chemistry department. The affinity of newly synthesized ligands is assessed by radioligand receptor binding assays. Based on our previous studies, 2-phenyl-5-oxo-7-methyl-1,3,4-oxadiazolo[a,2,3]-pyrimid...

Hepatitis C Virus (HCV) encodes two envelope glycoproteins, E1 and E2. Our previous work selected a specific aptamer ZE2, which could bind to E2 with high affinity, with a great potential for developing new molecular probes as an early diagnostic reagents or therapeutic drugs targeting HCV. In this study, the binding sites between E2 and aptamer ZE2 were further explored. E2 was truncated to 15...

Protein specific aptamers are highly applicable affinity ligands in different fields of research and clinical applications. They have been developed against various targets, in particular, bio-macromolecules such as proteins. Among human proteins, the coagulation factors are the most attractive targets for aptamer selection and their specific aptamers had valuable characteristics in therapeutic...