Studies on the interaction between promethazine and human serum albumin in the presence of flavonoids by spectroscopic and molecular modeling techniques

He, Lihua; Wang, Zhixin; Wang, Yongxia; Liu, Xian-Ping; Yang, Yanjie; Gao, Yanping; Wang, Xin; Liu, Bin

doi:10.1016/j.colsurfb.2016.06.001

Cited by 34 publications

(8 citation statements)

References 65 publications

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“…Nowadays, investigations on the interaction between flavonoids and proteins garner great interest [ 18 , 19 , 20 ]. As one of the most abundant proteins in the circulatory system, serum albumins are the major transport protein in blood and can reversibly bind to small molecules like fatty acids, amino acids, drugs, and inorganic ions [ 21 ].…”

Section: Introductionmentioning

confidence: 99%

Molecular Structure–Affinity Relationship of Flavonoids in Lotus Leaf (Nelumbo nucifera Gaertn.) on Binding to Human Serum Albumin and Bovine Serum Albumin by Spectroscopic Method

Tang

Liu

2017

Molecules

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Lotus leaf has gained growing popularity as an ingredient in herbal formulations due to its various activities. As main functional components of lotus leaf, the difference in structure of flavonoids affected their binding properties and activities. In this paper, the existence of 11 flavonoids in lotus leaf extract was confirmed by High Performance Liquid Chromatography (HPLC) analysis and 11 flavonoids showed various contents in lotus leaf. The interactions between lotus leaf extract and two kinds of serum albumins (human serum albumin (HSA) and bovine serum albumin (BSA)) were investigated by spectroscopic methods. Based on the fluorescence quenching, the interactions between these flavonoids and serum albumins were further checked in detail. The relationship between the molecular properties of flavonoids and their affinities for serum albumins were analyzed and compared. The hydroxylation on 3 and 3’ position increased the affinities for serum albumins. Moreover, both of the methylation on 3’ position of quercetin and the C2=C3 double bond of apigenin and quercetin decreased the affinities for HSA and BSA. The glycosylation lowered the affinities for HSA and BSA depending on the type of sugar moiety. It revealed that the hydrogen bond force played an important role in binding flavonoids to HSA and BSA.

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Section: Introductionmentioning

confidence: 99%

Molecular Structure–Affinity Relationship of Flavonoids in Lotus Leaf (Nelumbo nucifera Gaertn.) on Binding to Human Serum Albumin and Bovine Serum Albumin by Spectroscopic Method

Tang

Liu

2017

Molecules

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“…HSA has previously been co-crystallised with several ligands. It has been reported that AMT binds to both site 1 and 2 of HSA, while PMT only binds to site 1 and IMP shows a preference for site 2 [35][36][37] . Diclofenac is one of the drugs that closely resemble the cationic ligands binding in the small cavity in site 1, where AMT and PMT docked, in an orientation similar to diclofenac (Figure 1).…”

Section: Resultsmentioning

confidence: 99%

Morphological changes in human serum albumin in the presence of cationic amphiphilic drugs

et al. 2018

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“…[8] Characterizing the site within HSA to which drugs bind is of particular relevance, since drug-drug interactions may occur as a consequence of competition between co-administered drugs. [10,11]…”

Section: Accepted Manuscriptmentioning

confidence: 99%

Stability and plasmatic protein binding of novel zidovudine prodrugs: Targeting site ii of human serum albumin

Schenfeld

Ribone

Quevedo

2018

European Journal of Pharmaceutical Sciences

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Despite its vastly demonstrated clinical efficacy, zidovudine (AZT) exhibits several suboptimal pharmacokinetic properties. In particular, its short plasmatic half-life (t ~ 1 h) is related to its low bound fraction to whole plasmatic proteins and in particular to human serum albumin (HSA). The design of prodrugs constitutes a promising strategy to enhance AZT pharmacokinetic properties, including its affinity for HSA. Recently, we reported the synthesis and chemical stability evaluation of three novel prodrugs of AZT obtained by derivatization with dicarboxylic acids (1-3). In this work, we present the design, synthesis and evaluation of chemical and enzymatic stabilities of a novel series of double prodrugs of AZT obtained by derivatization of 1-3 with a methylated l-phenylalanine moiety (4-6). In addition, the plasmatic protein binding properties were studied both by experimental and theoretical techniques. Prodrugs 4-6 were found to be relatively stable at pH 7.4 (t between 4.1 and 57.8 h), while also demonstrated adequate stabilities in human plasma at 37 °C (t between 1.0 and 2.1 h). Also, prodrugs 4-6 were able to regenerate AZT at a rate that depended on the length of the alkyl chain in 1-3. Additionally, 4-6 exhibited a significantly increased binding to plasmatic proteins (between 52.1 and 72.5%) with respect to AZT (12%) and 1-3 (between 26 and 34%). It is noteworthy that the displacement experiments with HSA site I and II markers, demonstrated that 4-6 bound to a different site than that of AZT and 1-3. Molecular modeling studies (i.e. molecular docking and free energy of binding analysis) were applied to shed light at an atomistic level on the pharmacodynamic properties driving the interaction of 4-6 with HSA. Overall, the present work provides a state of the art contribution to the design and development of novel prodrugs of AZT with optimized pharmacokinetic properties.

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Studies on the interaction between promethazine and human serum albumin in the presence of flavonoids by spectroscopic and molecular modeling techniques

Cited by 34 publications

References 65 publications

Molecular Structure–Affinity Relationship of Flavonoids in Lotus Leaf (Nelumbo nucifera Gaertn.) on Binding to Human Serum Albumin and Bovine Serum Albumin by Spectroscopic Method

Molecular Structure–Affinity Relationship of Flavonoids in Lotus Leaf (Nelumbo nucifera Gaertn.) on Binding to Human Serum Albumin and Bovine Serum Albumin by Spectroscopic Method

Morphological changes in human serum albumin in the presence of cationic amphiphilic drugs

Stability and plasmatic protein binding of novel zidovudine prodrugs: Targeting site ii of human serum albumin

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