High-Performance affinity chromatographic studies of repaglinide and nateglinide interactions with normal and glyoxal- or methylglyoxal-modified human albumin serum

Ovbude, Susan T.; Tao, Pingyang; Zhao, Li; Hage, David S.

doi:10.1016/j.jpba.2021.114097

Cited by 11 publications

(23 citation statements)

References 22 publications

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“…Generally, aromatic carboxylic acids with a peripheric negative charge, that is distantly located from the hydrophobic centre, are lodged in the FA4 site [30]. Our data are in agreement with previous biochemical studies reporting that the majority of contraindicated drugs knowns to have adverse effects when co-administered with GEM appear to bind either or both Sudlow's binding sites I and II [36][37][38][39][40]. Overall, the protein complex HSA-GEM was superimposed well with that of other well-known HSA-drug binding complexes examined here.…”

Section: Discussionsupporting

confidence: 92%

Structural Analysis of Human Serum Albumin in Complex with the Fibrate Drug Gemfibrozil

Liberi

Linciano

Moro

et al. 2022

IJMS

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Gemfibrozil (GEM) is an orally administered lipid-regulating fibrate derivative drug sold under the brand name Lopid®, among others. Since its approval in the early 80s, GEM has been largely applied to treat hypertriglyceridemia and other disorders of lipid metabolism. Though generally well tolerated, GEM can alter the distribution and the free, active concentration of some co-administered drugs, leading to adverse effects. Most of them appear to be related to the ability of GEM to bind with high affinity human serum albumin (HSA), the major drug-carrier protein in blood plasma. Here, we report the crystal structure of HSA in complex with GEM. Two binding sites have been identified, namely Sudlow’s binding sites I (FA7) and II (FA3–FA4). A comparison of the crystal structure of HSA in complex with GEM with those of other previously described HSA–drug complexes enabled us to appreciate the analogies and differences in their respective binding modes. The elucidation of the molecular interaction between GEM and HSA might offer the basis for the development of novel GEM derivatives that can be safely and synergistically co-administered with other drugs, enabling augmented therapeutic efficacies.

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Section: Discussionsupporting

confidence: 92%

Structural Analysis of Human Serum Albumin in Complex with the Fibrate Drug Gemfibrozil

Liberi

Linciano

Moro

et al. 2022

IJMS

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“…The microcolumns used in this study showed consistent retention (<5% variation) over 600 sample injections or application cycles and 6 months of use. This degree of stability agrees with that seen previously for similar HSA supports and microcolumns [7–10].…”

Section: Methodssupporting

confidence: 92%

“…Equations ( 1) and ( 2) both gave reasonable fits to the data for glycated HSA; however, the two-site model gave a better overall fit than the one-site model. The same trend has been noted in prior work with repaglinide and normal HSA [8]. For instance, a slightly higher correlation coefficient (r) was obtained for the two-site versus one-site model for all supports containing glycated HSA, with values of F I G U R E 2 Frontal analysis plots for (A) two-site and (B) one-site models for the overall binding of repaglinide to a column containing glycated human serum albumin (gHSA2).…”

Section: Studies By Frontal Analysis To Examine Overall Drug-protein ...supporting

confidence: 85%

“…Portions of the glycated and normal HSA were immobilized by the Schiff base method onto diol-bonded Nucleosil Si-300 silica [29,33]. This immobilization scheme has been shown in many prior reports to provide supports that are a good model for the drug-binding properties of the soluble forms of normal HSA and glycated HSA [1,2,[7][8][9][10][21][22][23][24]. The Schiff base method was also utilized to prepare a control support, to which no normal HSA or glycated HSA was added during the immobilization step.…”

Section: Preparation Of Glycated Hsa Supports and Microcolumnsmentioning

confidence: 99%

“…These solutions were filtered and degassed for 20 min before use and were stored at 4 • C. The solutions of L-tryptophan were prepared fresh daily, and the solutions containing R-warfarin were prepared and used within four weeks [7][8][9][10]. All chromatographic studies were carried out at 37 • C and 0.50 ml/min (i.e., a flow rate found in prior work with similar microcolumns to give retention factors and breakthrough times independent of the injection flow rate) [7][8][9][10]. The backpressures of the microcolumns were typically 300 psi (3.0 MPa) or less under these conditions [7][8][9][10].…”

Section: Chromatographic Conditionsmentioning

confidence: 99%

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Characterization of binding by repaglinide and nateglinide with glycated human serum albumin using high‐performance affinity microcolumns

Ovbude

Tao

Zhao

et al. 2022

J of Separation Science

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High-performance affinity microcolumns were used to characterize binding by the anti-diabetic drugs repaglinide and nateglinide with normal and glycated forms of human serum albumin. The microcolumns contained only nmol amounts of protein and provided a detailed analysis of these drug interactions with good precision and in a matter of minutes per experiment. The overall binding by repaglinide to normal and glycated albumin fits a model with two types of binding sites: a set of one or two moderate-to-high affinity regions and a larger set of weaker regions with association equilibrium constants of ∼10 5 and 10 3 M −1 , respectively, at pH 7.4 and 37 • C. Competition studies gave site-specific association constants for repaglinide and nateglinide at Sudlow site I of 4.2 × 10 4 and 5.0 × 10 4 M −1 for normal albumin, with a decrease of 26%-30% being seen for nateglinide with glycated albumin and no significant change being noted for repaglinide. At Sudlow site II, repaglinide and nateglinide had association constants for normal albumin of 6.1 × 10 4 and 7.1 × 10 5 M −1 , with glycated albumin giving an increase in the association constant at this site for repaglinide of 1.6-to 1.8-fold and a decrease for nateglinide of 51%-58%.

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Design, synthesis, antibacterial evaluation of isopropylamine linked with different substituted phenol and piperazine novel derivatives

Wang,

Li,

Zhu

et al. 2024

Pest Management Science

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BACKGROUNDXanthomonas oryzae pv. oryzae (Xoo) is often considered one of the most destructive bacterial pathogens causing bacterial leaf blight (BLB), resulting in significant yield and cost losses in rice. In this study, a series of novel derivatives containing the isopropanolamine moiety linked to various substituted phenols and piperazines were designed, synthesized and screened.RESULTSAntibacterial activity results showed that most compounds had good inhibitory effects on Xoo, among which compound W2 (EC50 = 2.74 μg mL−1) exhibited the most excellent inhibitory activity, and W2 also had a certain curative effect (35.89%) on rice compared to thiodiazole copper (TC) (21.57%). Scanning electron microscopy (SEM) results indicated that compound W2 could cause rupture of the Xoo cell membrane. Subsequently, proteomics and quantitative real‐time polymerase chain reaction revealed that compound W2 affected the physiological processes of Xoo and may exert antibacterial activity by targeting the two‐component system pathway. Interestingly, W2 upregulated Xoo's methyltransferase to impact on its pathogenicity.CONCLUSIONThe present study offers a promising phenolic‐piperazine‐sopropanolamine compound as an innovative antibacterial strategy by specifically targeting the two‐component system pathway and inducing upregulation of methyltransferase to effectively impact Xoo's pathogenicity. © 2024 Society of Chemical Industry.

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High-Performance affinity chromatographic studies of repaglinide and nateglinide interactions with normal and glyoxal- or methylglyoxal-modified human albumin serum

Cited by 11 publications

References 22 publications

Structural Analysis of Human Serum Albumin in Complex with the Fibrate Drug Gemfibrozil

Structural Analysis of Human Serum Albumin in Complex with the Fibrate Drug Gemfibrozil

Characterization of binding by repaglinide and nateglinide with glycated human serum albumin using high‐performance affinity microcolumns

Design, synthesis, antibacterial evaluation of isopropylamine linked with different substituted phenol and piperazine novel derivatives

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