A comparative analysis on the binding characteristics of various mammalian albumins towards a multitherapeutic agent, pinostrobin

Feroz, Shevin Rizal; Sumi, Rumana A.; Malek, Sri Nurestri Abd; Tayyab, Saad

doi:10.1538/expanim.14-0053

Cited by 8 publications

(4 citation statements)

References 38 publications

(47 reference statements)

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“…Furthermore, an anthracene derivative was reported to show different behaviors in the binding to PSA, BSA, HSA, SSA, and RSA . A therapeutic agent, pinostrobin, also exhibited differences in hydrophobic interaction-based binding behaviors to PSA, BSA, HSA, GSA, SSA, and RSA . Therefore, the properties of the C-terminal region and the hydrophobic region on PSA might influence the selectivity.…”

Section: Resultsmentioning

confidence: 99%

“…65 A therapeutic agent, pinostrobin, also exhibited differences in hydrophobic interaction-based binding behaviors to PSA, BSA, HSA, GSA, SSA, and RSA. 66 Therefore, the properties of the C-terminal region and the hydrophobic region on PSA might influence the selectivity. In contrast, PSA selectivity was not observed in NIP-NGs, where the selectivity factors of BSA, HSA, GSA, SSA, and RSA at 1000 μg/mL were estimated to be 1.00, 1.41, 1.14, 0.83, and 1.46, respectively (Figure 3b).…”

Section: ■ Results and Discussionmentioning

confidence: 99%

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Molecularly Imprinted Nanogels Capable of Porcine Serum Albumin Detection in Raw Meat Extract for Halal Food Control

et al. 2020

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Accurate, simple, and valuable analytical methods for detection of food contamination are rapidly expanding to evaluate the validity of food product quality because of ethnic considerations and food safety. Herein molecularly imprinted nanogels (MIP-NGs), capable of porcine serum albumin (PSA) recognition, were prepared as artificial molecular recognition elements. The MIP-NGs were immobilized on a quartz crystal microbalance (QCM) sensor for detection of pork contamination in real beef extract samples. The MIP-NGs-based QCM sensor showed high affinity and excellent selectivity toward PSA compared to reference serum albumins from five different animals. The high PSA specificity of MIP-NGs led to the detection of pork contamination with a detection limit of 1% (v/v) in real beef extract samples. We believe the artificial molecular recognition materials prepared by molecular imprinting are a promising candidate for halal food control.

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Section: Resultsmentioning

confidence: 99%

Section: ■ Results and Discussionmentioning

confidence: 99%

Molecularly Imprinted Nanogels Capable of Porcine Serum Albumin Detection in Raw Meat Extract for Halal Food Control

et al. 2020

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“…In a crystal structure of the equine albumin complex with cefaclor, cefaclor molecules are bound between subdomains IA and IB and between subdomains IIA, IIB, and IIIA (PDB ID: 7Q4X). It is well-known that the degree of albumin binding for an agent and its binding position vary depending on the species, − thus whether the binding sites of cefaclor in HSA are identical to that in equine albumin would need to be clarified. In addition, cefaclor shows low plasma protein binding and low binding affinity to HSA, and the pharmacokinetic significance of such low plasma protein binding remains unclear.…”

Section: Discussionmentioning

confidence: 99%

Interaction of Cephalosporins with Human Serum Albumin: A Structural Study

Kawai,

Yamasaki,

Otagiri

et al. 2024

J. Med. Chem.

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Modification of the R1 and R2 side chain structures has been used as the main strategy to expand the spectrum of cephalosporins and impart resistance to hydrolysis by β-lactamases. These structural modifications also result in a wide range of plasma protein binding, especially with human serum albumin (HSA). Here, we determined the crystal structures of the HSA complexes with two clinically important cephalosporins, ceftriaxone and cefazolin, and evaluated the binding of cephalosporin to HSA by susceptibility testing and competitive binding assay. Ceftriaxone and cefazolin bind to subdomain IB of HSA, and their cephem core structures are recognized by Arg117 of HSA. Tyr161 of HSA changes its rotamer depending on the cephalosporin, resulting in alterations of the cavity shape occupied by the R2 side chain of cephalosporins. These findings provide structural insight into the mechanisms underlying the HSA binding of cephalosporins.

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“…Several studies done concerning the binding of drugs to albumins from several species have been reported. [28][29][30][31][32][33][34][35] Panjehshahin et al 30 hypothesized that bovine, dog, horse, and sheep albumins contain binding sites that function similar to sites I and II of human albumin. However, they also implied that the binding sites for rat albumin are different from those of other albumins.…”

Section: Introductionmentioning

confidence: 99%

Species Differences in the Binding of Sodium 4-Phenylbutyrate to Serum Albumin

Yamasaki

Enokida

Taguchi

et al. 2017

Journal of Pharmaceutical Sciences

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Sodium 4-phenylbutyrate (PB) is clinically used as a drug for treating urea cycle disorders. Recent research has shown that PB also has other pharmacologic activities, suggesting that it has the potential for use as a drug for treating other disorders. In the process of drug development, preclinical testing using experimental animals is necessary to verify the efficacy and safety of PB. Although the binding of PB to human albumin has been studied, our knowledge of its binding to albumin from the other animal species is extremely limited. To address this issue, we characterized the binding of PB to albumin from several species (human, bovine, rabbit, and rat). The results indicated that PB interacts with 1 high-affinity site of albumin from these species, which corresponds to site II of human albumin. The affinities of PB to human and bovine albumins were higher than those to rabbit and rat albumin, and that to rabbit albumin was the lowest. Binding and molecular docking studies using structurally related compounds of PB suggested that species differences in the affinity are attributed to differences in the structural feature of the PB-binding sites on albumins (e.g., charge distribution, hydrophobicity, shape, or size).

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A comparative analysis on the binding characteristics of various mammalian albumins towards a multitherapeutic agent, pinostrobin

Cited by 8 publications

References 38 publications

Molecularly Imprinted Nanogels Capable of Porcine Serum Albumin Detection in Raw Meat Extract for Halal Food Control

Molecularly Imprinted Nanogels Capable of Porcine Serum Albumin Detection in Raw Meat Extract for Halal Food Control

Interaction of Cephalosporins with Human Serum Albumin: A Structural Study

Species Differences in the Binding of Sodium 4-Phenylbutyrate to Serum Albumin

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