Quinolinesulfonamides: Interaction between bovine serum albumin, molecular docking analysis, and antiproliferative activity against human breast carcinoma cells

Marciniec, Krzysztof; Pawełczak, Bartosz; Latocha, Małgorzata; Sułkowski, Leszek; Maślankiewicz, Andrzej; Maciążek-Jurczyk, Małgorzata; Boryczka, Stanisław

doi:10.1080/00387010.2017.1383920

Cited by 3 publications

(6 citation statements)

References 31 publications

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“…Emission spectrum is a sensitive detector of changes within fluorophores, which tyrosines (Tyrs) and tryptophans (Trps) are [8,13,14,17]. At λ ex = 280 nm both Tyrs and Trps are excited, while at λ ex = 295 nm only Trps are [8,12,13].…”

Section: Discussionmentioning

confidence: 99%

“…BSA, which structurally is the most similar to HSA, contains in the amino acid sequence two Trps (Trp135 and Trp214), instead of only one, Trp214, in HSA [2,12,13]. This structural dissimilarity between the two albumins enables spectroscopic information to be obtained from both subdomains IIA and IB when BSA is studied [9,12,13,17].…”

Section: Discussionmentioning

confidence: 99%

“…Among serum albumins of other species, the structure of bovine serum albumin (BSA) is the most similar to HSA [9,12]. The amino acid sequences of HSA and BSA are 76% homologous [9,17]. From a spectroscopic point of view, tryptophanyl residues, which are fluorophores, are important.…”

Section: Introductionmentioning

confidence: 99%

“…Trp135 is located in subdomain IB, while Trp214 is located in subdomain IIA [11]. This dissimilarity between HSA and BSA enables additional spectroscopic observations [17,18].…”

Section: Introductionmentioning

confidence: 99%

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Stability of spectrofluorimetric spectra of hematoporphyrin–serum albumin complexes: in vitro study

Sułkowski¹,

Matyja²,

Osuch³

et al. 2021

Arch Med Sci Civil Dis

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IntroductionHematoporphyrin is a photosensitizer used in photodynamic therapy of various malignant diseases. It is carried to the cancer tissue by serum albumins. Spectrofluorimetric spectra of hematoporphyrin–serum albumin complexes were examined in vitro.Material and methodsThe chemicals were: hematoporphyrin, human serum albumin and bovine serum albumin. The spectra were recorded on a Kontron SFM-25 Instrument AG at two excitation wavelengths: ex = 280 nm and ex = 295 nm. The spectra of hematoporphyrin 1.5 × 10–5 M as well as spectra of complexes of hematoporphyrin–human serum albumin (1.5 × 10–5 M Hp – 1.25 × 10–6 M HSA) and hematoporphyrin–bovine serum albumin (1.5 × 10–5 M Hp – 3.5 × 10–7 M BSA) were recorded repetitively for 8 days and compared to the initial spectrum.ResultsFormation of a complex with human serum albumin extends the stability of the hematoporphyrin spectrum. This extension is greater at excitation ex = 295 nm. Different stability of complexes with bovine and human serum albumins most likely does not result from an actual lower stability of bovine serum albumin complexes, but from the fact that dissimilarity in the structure of both albumins enables additional spectroscopic observations within subdomain IB in the bovine serum albumin molecule.ConclusionsSpectrofluorimetric spectra are stable longer when hematoporphyrin forms a complex with human serum albumin. The present data may be important for understanding the mechanism of hematoporphyrin transportation to the target cancer tissue and effectiveness of photodynamic therapy.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

“…Trp135 is located in subdomain IB, while Trp214 is located in subdomain IIA [11]. This dissimilarity between HSA and BSA enables additional spectroscopic observations [17,18].…”

Section: Introductionmentioning

confidence: 99%

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Stability of spectrofluorimetric spectra of hematoporphyrin–serum albumin complexes: in vitro study

Sułkowski¹,

Matyja²,

Osuch³

et al. 2021

Arch Med Sci Civil Dis

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“…Exogenous ligands are primarily drugs (e.g. salicylates, sulfonamides, antibiotics) and contrast agents, including photosensitizers [22][23][24][25]. The complex formed between ligand and albumin protects the ligand against oxidation, reduces its toxicity, increases its solubility in the serum and therefore improves its transport [26].…”

Section: Introductionmentioning

confidence: 99%

Hematoporphyrin binding sites on human serum albumin

Sułkowski¹,

Osuch²,

Matyja³

et al. 2020

Arch Med Sci Civil Dis

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Introduction: Photodynamic therapy is a minimally invasive clinical treatment modality for a variety of premalignant and malignant conditions combining a photosensitizing drug, oxygen and light irradiation. Hematoporphyrin is an organic photosensitizer, which mediates inhibition of endothelial cell proliferation and induces apoptosis. Human serum albumin is an endogenous drug carrier for hematoporphyrin. The present study aimed to investigate the hematoporphyrin binding to human serum albumin, which is its transport protein. Material and methods: The chemical reagents were hematoporphyrin (Hp), human serum albumin (HSA) and bovine serum albumin (BSA). In the experiment two techniques were used: spectrofluorimetry and UV-Vis absorption spectrophotometry. Results: The binding sites for Hp were identified in the tertiary structure of HSA by fluorescence quenching technique. The experiment with BSA delivered additional data on Hp-albumin interactions close to Trp135. The participation of tyrosyl residues apart from tryptophanyl ones was discussed. A decrease of the polarity in the binding sites, testifying to possible hydrogen bonding in the binding sites, was also described. The binding and quenching constants Hp-HSA and Hp-BSA were determined as well as the number of binding sites. Conclusions: Hp locates in subdomain IIA in the tertiary structure of HSA. The location in subdomain I close to Trp135 is also possible. Hp is also able to interact within tyrosyl residues.

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Recent Advances in Biological Active Sulfonamide based Hybrid Compounds Part A: Two-Component Sulfonamide Hybrids

Ghomashi

Aghaei

et al. 2023

CMC

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Sulfonamides constitute an important class of drugs, with many types of pharmacological agents possessing antibacterial, anti-carbonic anhydrase, anti-obesity, diuretic, hypoglycemic, antithyroid, antitumor, and anti-neuropathic pain activities. The sulfonamides have the general formula R-SO2NHR', in which the functional group is bound to an aromatic, heterocycle, aliphatic, and so on. The nature of the R and R' moiety is variable, starting with hydrogen and ranging to a variety of moieties incorporating organic compounds such as coumarin, isoxazole, tetrazole, pyrazole, pyrrole, and so many other pharmaceutical active scaffolds that lead to a considerable range of hybrids named as sulfonamide hybrids. Part A of this review presents the most recent advances in designing and developing two-component sulfonamide hybrids containing coumarin, indole, quinoline, isoquinoline, chalcone, pyrazole/pyrazoline, quinazoline, pyrimidine, thiazole, benzothiazole, and pyridine between 2015 and 2020. Specifically, the authors review the scientific reports on the synthesis and biological activity of this kind of hybrid agent.

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Quinolinesulfonamides: Interaction between bovine serum albumin, molecular docking analysis, and antiproliferative activity against human breast carcinoma cells

Cited by 3 publications

References 31 publications

Stability of spectrofluorimetric spectra of hematoporphyrin–serum albumin complexes: in vitro study

Stability of spectrofluorimetric spectra of hematoporphyrin–serum albumin complexes: in vitro study

Hematoporphyrin binding sites on human serum albumin

Recent Advances in Biological Active Sulfonamide based Hybrid Compounds Part A: Two-Component Sulfonamide Hybrids

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