Biomolecular interactions and binding dynamics of tyrosine kinase inhibitor erdafitinib, with human serum albumin

Amir, Mohd; Qureshi, Mohd Aamir; Javed, Saleem

doi:10.1080/07391102.2020.1772880

Cited by 29 publications

(10 citation statements)

References 91 publications

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“…Stern–Volmer quenching constant (K SV ) for binding trans -resveratrol with HSA was calculated according to Eq. ( 1 ) 25 . There is linearity between the concentration of T-res (Q) and F 0 /F, as shown in Fig.…”

Section: Resultsmentioning

confidence: 99%

“…3 a, if we look at the F 0 /F vs Q plot at 298.15 K, at a higher concentration of trans -resveratrol, the F 0 /F vs Q plot is shifted towards y axis, envisaging a mixed type of fluorescence quenching mechanism at 298.15 K, however, the plot shows the complete straight line at 303.15 and 308.15 K. The major contribution is for static nature of fluorescence quenching since the K SV value decreases with increase in the temperature Further confirmation of the static quenching mechanism was done by calculating the bimolecular quenching constant (K q ) using Eq. ( 3 ) 25 of the “ Methods ” section. The numerical value of K q obtained at three different temperatures, as shown in Table 1 , is greater than the maximum scattering collision constant whose value is 2 × 10 10 M −1 s −1 , thus confirming the existence of static quenching and ground-state complex formation between HSA and trans -resveratrol 24 , 27 .…”

Section: Resultsmentioning

confidence: 99%

“…The binding constant (K b ) was calculated at three different temperatures, viz 298.15, 303.15, and 308.15 K using Eq. ( 4 ) 25 , 32 , mentioned in the “ Methods ” section. The plot of log (F 0 − F)/F versus log (Q) is shown in Fig.…”

Section: Resultsmentioning

confidence: 99%

See 2 more Smart Citations

Investigating binding dynamics of trans resveratrol to HSA for an efficient displacement of aflatoxin B1 using spectroscopy and molecular simulation

Qureshi

Javed

2022

Sci Rep

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Resveratrol is a polyphenol belonging to the class stilbenes. The active and stable form of resveratrol is trans-resveratrol. This polyphenol is bestowed with numerous biological properties. Aflatoxin B1 is a hepato-carcinogen and mutagen that is produced by Aspergillus species. In this study, the interaction of trans-resveratrol with HSA followed by competitive dislodging of AFB1 from HSA by trans-resveratrol has been investigated using spectroscopic studies. The UV-absorption studies revealed ground state complex formation between HSA and trans-resveratrol. Trans-resveratrol binds strongly to HSA with the binding constant of ~ 107 M−1 to a single binding site (n = 1.58), at 298.15 K. The Stern–Volmer quenching constant was calculated as 7.83 × 104 M−1 at 298.15 K, suggesting strong fluorescence quenching ability of trans-resveratrol. Site markers displacement assay projected subdomain IIA as the binding site of trans-resveratrol to HSA. The molecular docking approach envisages the amino acid residues involved in the formation of the binding pocket. As confirmed from the site marker displacement assays, both trans-resveratrol and AFB1 binds to HSA in the same binding site, subdomain IIA. The study explores the ability of trans-resveratrol to displace AFB1 from the HSA-AFB1 complex, thereby affecting the toxicokinetic behavior of AFB1 associated with AFB1 exposure.

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Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

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Investigating binding dynamics of trans resveratrol to HSA for an efficient displacement of aflatoxin B1 using spectroscopy and molecular simulation

Qureshi

Javed

2022

Sci Rep

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“…TKIs are small molecules that are used to treat a wide range of malignancies, including leukemia and solid tumors (Amir et al, 2020). TKIs have been developed as a targeted treatment for BCR-ABL1 kinase activity suppression (Cilloni and Saglio, 2012).…”

Section: Targeted Therapy For CML Using Tyrosine Kinase Inhibitors Current Use Of Tkis For Cml Treatmentmentioning

confidence: 99%

A Review on the Therapeutic Role of TKIs in Case of CML in Combination With Epigenetic Drugs

Amir

Javed

2021

Front. Genet.

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Chronic myeloid leukemia is a malignancy of bone marrow that affects white blood cells. There is strong evidence that disease progression, treatment responses, and overall clinical outcomes of CML patients are influenced by the accumulation of other genetic and epigenetic abnormalities, rather than only the BCR/ABL1 oncoprotein. Both genetic and epigenetic factors influence the efficacy of CML treatment strategies. Targeted medicines known as tyrosine-kinase inhibitors have dramatically improved long-term survival rates in CML patients during the previous 2 decades. When compared to earlier chemotherapy treatments, these drugs have revolutionized CML treatment and allowed most people to live longer lives. Although epigenetic inhibitors’ activity is disrupted in many cancers, including CML, but when combined with TKI, they may offer potential therapeutic strategies for the treatment of CML cells. The epigenetics of tyrosine kinase inhibitors and resistance to them is being studied, with a particular focus on imatinib, which is used to treat CML. In addition, the use of epigenetic drugs in conjunction with TKIs has been discussed. Resistance to TKIs is still a problem in curing the disease, necessitating the development of new therapies. This study focused on epigenetic pathways involved in CML pathogenesis and tumor cell resistance to TKIs, both of which contribute to leukemic clone breakout and proliferation.

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“…The interactions between proteins are not only affected by pH and temperature, but also by exogenous compounds [ 3 ]. Researchers have used spectroscopy to study the interaction of the tyrosine kinase inhibitors erdafitinib and vandetanib with human serum albumin, and proposed that the introduction of the drug affects the hydrophobic domain of the protein, especially the microenvironment around tryptophan [ 4 , 5 ]. In addition, Wani et al, in their study on the interaction of the tyrosine kinase inhibitor erlotinib with BSA [ 6 ], proposed that the presence of the drug affects the formation of protein complexes.…”

Section: Introductionmentioning

confidence: 99%

Investigating the Effect of Tyrosine Kinase Inhibitors on the Interaction between Human Serum Albumin by Atomic Force Microscopy

Wang

2022

Biomolecules

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It is important for elucidating the regulation mechanism of life activities, as well as for the prevention, diagnosis, and drug design of diseases, to study protein–protein interactions (PPIs). Here, we investigated the interactions of human serum albumin (HSA) in the presence of tyrosine kinase inhibitors (TKIs: imatinib, nilotinib, dasatinib, bosutinib, and ponatinib) using atomic force microscopy (AFM). The distribution of rupture events including the specific interaction force Fi and the non-specific interaction force F0 between HSA pairs was analyzed. Based on the force measurements, Fi and F0 between HSA pairs in the control experiment were calculated to be 47 ± 1.5 and 116.1 ± 1.3 pN. However, Fi was significantly decreased in TKIs, while F0 was slightly decreased. By measuring the rupture forces at various loading rates and according to the Bell equation, the kinetic parameters of the complexes were investigated in greater detail. Molecular docking was used as a complementary means by which to explore the force of this effect. The whole measurements indicated that TKIs influenced PPIs in a variety of ways, among which hydrogen bonding and hydrophobic interactions were the most important. In conclusion, these outcomes give us a better insight into the mechanisms of PPIs when there are exogenous compounds present as well as in different liquid environments.

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Biomolecular interactions and binding dynamics of tyrosine kinase inhibitor erdafitinib, with human serum albumin

Cited by 29 publications

References 91 publications

Investigating binding dynamics of trans resveratrol to HSA for an efficient displacement of aflatoxin B1 using spectroscopy and molecular simulation

Investigating binding dynamics of trans resveratrol to HSA for an efficient displacement of aflatoxin B1 using spectroscopy and molecular simulation

A Review on the Therapeutic Role of TKIs in Case of CML in Combination With Epigenetic Drugs

Investigating the Effect of Tyrosine Kinase Inhibitors on the Interaction between Human Serum Albumin by Atomic Force Microscopy

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