Interaction of lafutidine in binding to human serum albumin in gastric ulcer therapy: STD-NMR, WaterLOGSY-NMR, NMR relaxation times, Tr-NOESY, molecule docking, and spectroscopic studies.
TL;DR: In this study, lafutidine (LAF) was used as a model compound to investigate the binding mechanism between antiulcer drugs and human serum albumin (HSA) through various techniques, including STD-NMR, WaterLOGSY-N MR, (1)H NMR relaxation times, tr-NOESY, molecule docking calculation, FT-IR spectroscopy, and CD spectroscopic.
About: This article is published in Archives of Biochemistry and Biophysics.The article was published on 2016-09-15. It has received 18 citations till now. The article focuses on the topics: Two-dimensional nuclear magnetic resonance spectroscopy & Antiulcer drug.
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TL;DR: In this review, microscale thermophoresis technology (MST) is presented as an analytical technique for characterizing biomolecular interactions and is found to be a powerful technique in quantitation of binding events based on the movement of molecules in microscopic temperature gradient.
83 citations
TL;DR: Examination of the interaction between Repaglinide and a model protein, bovine serum albumin, employing various spectroscopic, electrochemical and molecular docking methods revealed that RPG quenched the intensity of BSA through dynamic quenching mechanism.
62 citations
TL;DR: In this article , the authors examined the inducement of an interaction between two carrier proteins, human serum albumin (HSA) and human holo transferrin (HTF) within the presence of cyanidinin the form of binary and ternary systems, which was conducted by different spectroscopic, isothermal titration calorimetric (ITC), and molecular dynamics simulation techniques.
59 citations
TL;DR: The interactions of cinnamaldehyde (CNMA), a food perfume, and its major metabolite cinnamic acid (CA) with human serum albumin (HSA) were examined by multiple-spectroscopies and increased the knowledge regarding the safety and biological action of CNMA and CA.
55 citations
TL;DR: Several techniques that can be implemented to explore the conformational changes induced in serum albumin during the transport process are discussed and come up with data that are simple to interpret and give reliable information regarding the interaction between therapeutic molecules and proteins.
46 citations
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TL;DR: A nuclear magnetic resonance (NMR)-based method is described in which small organic molecules that bind to proximal subsites of a protein are identified, optimized, and linked together to produce high-affinity ligands and appears particularly useful in target-directed drug research.
Abstract: A nuclear magnetic resonance (NMR)-based method is described in which small organic molecules that bind to proximal subsites of a protein are identified, optimized, and linked together to produce high-affinity ligands. The approach is called "SAR by NMR" because structure-activity relationships (SAR) are obtained from NMR. With this technique, compounds with nanomolar affinities for the FK506 binding protein were rapidly discovered by tethering two ligands with micromolar affinities. The method reduces the amount of chemical synthesis and time required for the discovery of high-affinity ligands and appears particularly useful in target-directed drug research.
1,971 citations
Journal Article•
TL;DR: The binding of a number of fluorescent probe molecules to human serum albumin has been studied and changes in probe fluorescence were shown to be a result of competitive displacement by drugs.
Abstract: The binding of a number of fluorescent probe molecules to human serum albumin (HSA) has been studied. Small changes in the amino acid moiety of the dansylamino acids resulted in large changes in the binding of these compounds to HSA. It is suggested that electrostatic and dipolar forces play a role in the specificity and binding affinity of such compounds. Fluorescent probes which had one tight binding site were used for drug displacement studies. Changes in probe fluorescence were shown, by equilibrium dialysis and by fluorescence titrations, to be a result of competitive displacement by drugs. The pattern of displacement of probes by drugs enabled the identification of two specific drug binding sites. The relative affinity of drugs for these binding sites was measured by their ability to displace fluorescent probes specific for the sites. The method provides a rapid and simple means for detecting potential drug interactions based on competition for protein binding sites.
1,529 citations
TL;DR: Fast identification of binding activity directly from mixtures of potential ligands is possible with the NMR method described, which is based on saturation transfer to molecules in direct contact to a protein.
Abstract: Fast identification of binding activity directly from mixtures of potential ligands is possible with the NMR method described, which is based on saturation transfer to molecules in direct contact to a protein. In addition, the ligand's binding epitope is easily identified. High sensitivity and ease of use are the principal advantages of this method. The picture shows the normal 1D NMR spectrum of a mixture and the spectrum obtained by applying the STD method, which exclusively shows signals from molecules with binding affinity.
1,432 citations
Journal Article•
TL;DR: The specificity of the sites for particular drugs, even at high drug to albumin ratios, was established, and the specificity and characteristics of the two sites on human adult and neonatal sera were shown to be similar to those on crystalline HSA.
Abstract: The fluorescent probes 5-dimethylaminonaphthalene-1-sulfonamide and dansylsarcosine function as specific markers for two distinct binding sites for anionic drugs on human serum albumin (HSA). The binding of drugs to site I or II was detected by measuring the displacement of these probes. The results give an indication of some of the structural features required for binding at these sites. Stearic acid binding to HSA induced different conformational changes in the albumin at sites I and II, which were detected by changes in the fluorescence and/or strength of binding of probes specific for the two sites. This provides further evidence for qualitative differences between the two sites. The specificity of the sites for particular drugs, even at high drug to albumin ratios, was established, and the specificity and characteristics of the two sites on human adult and neonatal sera were shown to be similar to those on crystalline HSA.
1,360 citations
TL;DR: Analysis of STD NMR experiments performed under competitive conditions proved that the two saccharides studied bind at the same receptor site, thereby ruling out unspecific binding.
Abstract: A protocol based on saturation transfer difference (STD) NMR spectra was developed to characterize the binding interactions at an atom level, termed group epitope mapping (GEM). As an example we chose the well-studied system of galactose binding to the 120-kDa lectin Ricinus communis agglutinin I (RCA120). As ligands we used methyl β-d-galactoside and a biantennary decasaccharide. Analysis of the saturation transfer effects of methyl β-d-galactoside showed that the H2, H3, and H4 protons are saturated to the highest degree, giving evidence of their close proximity to protons of the RCA120 lectin. The direct interaction of the lectin with this region of the galactose is in excellent agreement with results obtained from the analysis of the binding specificities of many chemically modified galactose derivatives (Bhattacharyya, L.; Brewer, C. F. Eur. J. Biochem. 1988, 176, 207−212). This new NMR technique can identify the binding epitope of even complex ligands very quickly, which is a great improvement over ...
1,069 citations