Alteration of methotrexate binding to human serum albumin induced by oxidative stress. Spectroscopic comparative study

Maciążek-Jurczyk, Małgorzata; Sułkowska, Anna; Równicka-Zubik, J.

doi:10.1016/j.saa.2014.12.113

Cited by 18 publications

(13 citation statements)

References 43 publications

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“…The presence of intra-or intermolecular hydrogen bonding related to the deshielding effect is a factor that strongly influences the changes in chemical shifts of amino acid residues proton resonances. It points to a decrease of electron density in the surroundings of the mentioned group similar to that in Maciążek-Jurczyk et al's paper [16]. Modification of serum albumin tertiary structure can be explained by a downfield shift of gHSA resonance signals taking part in the hydrogen bonding.…”

Section: Tablesupporting

confidence: 71%

Alteration of human serum albumin tertiary structure induced by glycation. Spectroscopic study

Szkudlarek

Maciążek-Jurczyk

Chudzik

et al. 2016

Spectrochimica Acta Part A: Molecular and Biomolecular Spectros

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Section: Tablesupporting

confidence: 71%

Alteration of human serum albumin tertiary structure induced by glycation. Spectroscopic study

Szkudlarek

Maciążek-Jurczyk

Chudzik

et al. 2016

Spectrochimica Acta Part A: Molecular and Biomolecular Spectros

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“…Higher shift for glycated albumin indicates that the “fructation” of HSA decreases mobility of Trp-214 inducing changes of albumin conformation. Similarly, larger REES in case of modified-oxidized (oHSA, Δλ em = 39 nm) vs. non-modified (HSA, Δλ em = 4 nm) human serum albumin Maciążek-Jurczyk et al have observed [ 30 ]. As the authors mentioned, it points to the structural modifications in the hydrophobic pocket containing the tryptophanyl residue due to the oxidation process, which contribute to stiffening of the Trp-214 environment or/and limited access to the polar solvent.…”

Section: Resultsmentioning

confidence: 99%

“…Changes in glycated human serum albumin structure compare to non-glycated can be explained by an upfield shift of gHSA FRC resonance signals taking part in the intramolecular or intermolecular hydrogen bondings. Maciążek-Jurczyk et al [ 30 ] emphasized that a downfield shift resonance signals of oxidized HSA (oHSA) compare to non-modified HSA points to a decrease of electron density in the surroundings of amino acid residues such as tryptophan and cysteine.…”

Section: Resultsmentioning

confidence: 99%

In Vitro Investigation of the Interaction of Tolbutamide and Losartan with Human Serum Albumin in Hyperglycemia States

et al. 2017

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Serum albumin is exposed to numerous structural modifications which affect its stability and activity. Glycation is one of the processes leading to the loss of the original properties of the albumin and physiological function disorder. In terms of long lasting states of the hyperglycemia, Advanced Glycation End-products (AGEs) are formed. AGEs are responsible for cellular and tissue structure damage that cause the appearance of a number of health consequences and premature aging. The aim of the present study was to analyze the conformational changes of serum albumin by glycation—“fructation”—using multiple spectroscopic techniques, such as absorption (UV-Vis), fluorescence (SFM), circular dichroism (CD) and nuclear magnetic resonance (NMR) spectroscopy and evaluate of possible alteration of binding and competition between tolbutamide (TB, a first-generation sulfonylurea oral hypoglycemic drug) and losartan (LOS, an angiotensin II receptor (AT1) blocker used in hypertension (1st line with a coexisting diabetes)) in binding to non-glycated (HSA) and glycated (gHSAFRC) human serum albumin in high-affinity binding sites. The studies allowed us to indicate the structural alterations of human serum albumin as a result of fructose glycation. Changes in binding parameters, such as association (Ka) or Stern-Volmer (KSV) constants suggest that glycation increases the affinity of TB and LOS towards albumin and affects interactions between them. The process of albumin glycation influences the pharmacokinetics of drugs, thus monitored pharmacotherapy is reasonable in the case of diabetes and hypertension polypharmacy. This information may lead to the development of more effective drug treatments based on personalized medicine for patients with diabetes. Our studies suggest the validity of monitored polypharmacy of diabetes and coexisting diseases.

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“…The corresponding results at different temperatures are listed in Table . The value of K a at 298 K agrees with a previous result from Maciążek–Jurczyk et al, and the decreasing trend of binding constants ( K a and K b ) with increasing temperature was in accordance with K sv 's dependence on temperature as mentioned above.…”

Section: Resultsmentioning

confidence: 99%

Insights into the interaction of methotrexate and human serum albumin: A spectroscopic and molecular modeling approach

et al. 2017

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In this study, fluorescence spectroscopy and molecular modeling approaches were employed to investigate the binding of methotrexate to human serum albumin (HSA) under physiological conditions. From the mechanism, it was demonstrated that fluorescence quenching of HSA by methotrexate results from the formation of a methotrexate/HSA complex. Binding parameters calculated using the Stern-Volmer method and the Scatchard method showed that methotrexate binds to HSA with binding affinities in the order 10 L·mol . Thermodynamic parameter studies revealed that the binding reaction is spontaneous, and that hydrogen bonds and van der Waals interactions play a major role in the reaction. Site marker competitive displacement experiments and a molecular modeling approach demonstrated that methotrexate binds with appropriate affinity to site I (subdomain IIA) of HSA. Furthermore, we discuss some factors that influence methotrexate binding to HSA.

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Alteration of methotrexate binding to human serum albumin induced by oxidative stress. Spectroscopic comparative study

Cited by 18 publications

References 43 publications

Alteration of human serum albumin tertiary structure induced by glycation. Spectroscopic study

Alteration of human serum albumin tertiary structure induced by glycation. Spectroscopic study

In Vitro Investigation of the Interaction of Tolbutamide and Losartan with Human Serum Albumin in Hyperglycemia States

Insights into the interaction of methotrexate and human serum albumin: A spectroscopic and molecular modeling approach

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