Spectroscopic Studies on the Interaction between Tilorone and Human Serum Albumin

Under physiological conditions, in vitro interaction between the antiviral drug 2,7-bis[2-(diethylamino)ethoxy]-9-fluorenone dihydrochloride (Tilorone, TIL) and human serum albumin (HSA) was investigated at excitation wavelength 280 nm and at different temperatures (298 K and 313 K) by fluorescence emission spectroscopy. TIL showed a strong ability to quench the intrinsic fluorescence of HSA through a static quenching procedure. The binding constant is estimated as KA =7.19× 104L·mol-1 at 298 K. The enthalpy change (ΔHº) and entropy change (ΔSº) were derived to be negative values. A value of 1.63 nm for the average distance r between TIL (acceptor) and tryptophan residues of HSA (donor) was derived from the fluorescence resonance energy transfer.

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Spectroscopic Studies on the Interaction Between Novel Antiviral Drug Favipiravir and Serum Albumins

French-Ukrainian Journal of Chemistry ◽

10.17721/fujcv8i2p93-103 ◽

2020 ◽

Vol 8 (2) ◽

pp. 93-103

Author(s):

Alla Yegorova ◽

Yulia Scrypynets ◽

Georgy Maltsev ◽

Inna Leonenko ◽

Valery Antonovich ◽

...

Keyword(s):

Antiviral Drug ◽

Resonance Energy Transfer ◽

Fluorescence Emission ◽

Resonance Energy ◽

Binding Constants ◽

Spectroscopic Studies ◽

Excitation Wavelength ◽

Serum Albumins ◽

Different Temperatures

Under physiological conditions, in vitro interaction between favipiravir (FAV) and serum albumins (BSA/HSA) was investigated at excitation wavelength 280 nm and at different temperatures (298 K, 313 K) by fluorescence emission spectroscopy. The hydrogen bond, van der Waals forces and electrostatic interaction plays a major role in stabilizing the complex; the binding constants KA at different temperatures were calculated. The distance r between donor (BSA/HSA) and acceptor (FAV) was obtained according to fluorescence resonance energy transfer (1.55/1.90 nm for BSA/HSA-FAV systems). The effect of FAV on the conformation of BSA/HSA was analyzed using synchronous fluorescence spectroscopy and UV/vis absorption spectroscopy.

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Fluorescence Spectroscopic Studies of in vitro Interactions of Famotidine and Tapentadol Hydrochloride with Bovine Serum Albumin

Dhaka University Journal of Pharmaceutical Sciences ◽

10.3329/dujps.v15i1.29187 ◽

2016 ◽

Vol 15 (1) ◽

pp. 21-26

Author(s):

Md Rasal Hossain Khan ◽

Asma Rahman ◽

Md Zakir Sultan ◽

Md Zamil Sultan ◽

Mohammad A Rashid

Keyword(s):

Human Serum Albumin ◽

Bovine Serum Albumin ◽

Serum Albumin ◽

Sequence Homology ◽

Bovine Serum ◽

Emission Spectroscopy ◽

Fluorescence Emission ◽

Spectroscopic Studies ◽

In Vitro Interactions

The in vitro interactions of Famotidine (FT) and Tapentadol hydrochloride (TAP) with bovine serum albumin (BSA) have been studied by fluorescence emission spectroscopy under different conditions. Quenching constants were determined using the Stern-Volmer equation. Two moles FT bound with 1 mole of BSA at 298 K and 3 mole FT bound with 1 mole of BSA at 308 K in presence of TAP. BSA was used for the study as it shows approximately 76% sequence homology to human serum albumin (HSA).Dhaka Univ. J. Pharm. Sci. 15(1): 21-26, 2016 (June)

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Study on the interaction of ertugliflozin with human serum albumin in vitro by multispectroscopic methods, molecular docking, and molecular dynamics simulation

Spectrochimica Acta Part A Molecular and Biomolecular Spectroscopy ◽

10.1016/j.saa.2019.04.047 ◽

2019 ◽

Vol 219 ◽

pp. 83-90 ◽

Cited By ~ 14

Author(s):

Wenjing Wang ◽

Na Gan ◽

Qiaomei Sun ◽

Di Wu ◽

Ruixue Gan ◽

...

Keyword(s):

Molecular Dynamics ◽

Molecular Docking ◽

Molecular Dynamics Simulation ◽

Human Serum Albumin ◽

Serum Albumin ◽

Human Serum ◽

Dynamics Simulation

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Nof2206Probing the interaction of memantine, an important Alzheimer's drug, with human serum albumin: In silico and In vitro approach

Journal of Molecular Liquids ◽

10.1016/j.molliq.2021.116888 ◽

2021 ◽

pp. 116888

Author(s):

Fahad A. Alhumaydhi ◽

Mohammad Abdullah Aljasir ◽

Abdullah S.M. Aljohani ◽

Suliman A. Alsagaby ◽

Ameen S.S. Alwashmi ◽

...

Keyword(s):

Human Serum Albumin ◽

Serum Albumin ◽

Human Serum ◽

In Silico

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Synthesis and In Vitro Assessment of pH-Sensitive Human Serum Albumin Conjugates of Pirarubicin

Pharmaceuticals ◽

10.3390/ph14010022 ◽

2020 ◽

Vol 14 (1) ◽

pp. 22

Author(s):

Kenji Tsukigawa ◽

Shuhei Imoto ◽

Keishi Yamasaki ◽

Koji Nishi ◽

Toshihiko Tsutsumi ◽

...

Keyword(s):

Human Serum Albumin ◽

Serum Albumin ◽

Human Serum ◽

Coupling Reaction ◽

Synthetic Polymer ◽

Ph Sensitive ◽

Acidic Ph ◽

Polymer Conjugate ◽

Acidic Conditions

In a previous study, we reported on the development of a synthetic polymer conjugate of pirarubicin (THP) that was formed via an acid-labile hydrazone bond between the polymer and the THP. However, the synthetic polymer itself was non-biodegradable, which could lead to unexpected adverse effects. Human serum albumin (HSA), which has a high biocompatibility and good biodegradability, is also a potent carrier for delivering antitumor drugs. The objective of this study was to develop pH-sensitive HSA conjugates of THP (HSA-THP), and investigate the release of THP and the cytotoxicity under acidic conditions in vitro for further clinical development. HSA-THP was synthesized by conjugating maleimide hydrazone derivatives of THP with poly-thiolated HSA using 2-iminothiolane, via a thiol-maleimide coupling reaction. We synthesized two types of HSA-THP that contained different amounts of THP (HSA-THP2 and HSA-THP4). Free THP was released from both of the HSA conjugates more rapidly at an acidic pH, and the rates of release for HSA-THP2 and HSA-THP4 were similar. Moreover, both HSA-THPs exhibited a higher cytotoxicity at acidic pH than at neutral pH, which is consistent with the effective liberation of free THP under acidic conditions. These findings suggest that these types of HSA-THPs are promising candidates for further development.

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The in Vitro Anti-HIV Efficacy of Negatively Charged Human Serum Albumin Is Antagonized by Heparin

AIDS Research and Human Retroviruses ◽

10.1089/aid.1997.13.677 ◽

1997 ◽

Vol 13 (8) ◽

pp. 677-683 ◽

Cited By ~ 3

Author(s):

P.J. SWART ◽

C.S. SUN ◽

M.E. KUIPERS ◽

C. ASUNCION ◽

S. JOSEPHS ◽

...

Keyword(s):

Human Serum Albumin ◽

Serum Albumin ◽

Human Serum ◽

Anti Hiv

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Kinetic study of the photochemical changes of (ZZ)-bilirubin IX α bound to human serum albumin. Demonstration of (EZ)-bilirubin IX α as an intermediate in photochemical changes from (ZZ)-bilirubin IX α to (EZ)-cyclobilirubin IX α

Biochemical Journal ◽

10.1042/bj2260251 ◽

1985 ◽

Vol 226 (1) ◽

pp. 251-258 ◽

Cited By ~ 25

Author(s):

S Itoh ◽

S Onishi

Keyword(s):

Human Serum Albumin ◽

Serum Albumin ◽

Kinetic Study ◽

Human Serum ◽

Photochemical Reaction ◽

Relative Rate ◽

Significant Preference ◽

Geometrical Isomers ◽

Relative Rate Constants

The present study was performed to elucidate why the photochemical reaction of (ZZ)-bilirubin bound to human serum albumin is singularly selective, and only one of the two (EZ)- and (ZE)-bilirubins, the (ZE)-isomer, is produced. In a kinetic study of the photochemical reaction in vitro, the sum of the relative rate constants of photochemical transformation of (EZ)-bilirubin into both (EZ)-cyclobilirubin and (ZZ)-bilirubin, with a significant preference for the former, was proved to be considerably larger than that of the transformation of (ZZ)-bilirubin into (EZ)-bilirubin. Therefore only one of the geometrical isomers, namely (ZE)-bilirubin, is apparently formed. It was concluded that (EZ)-bilirubin photochemically undergoes (EZ)-cyclization, i.e. structural photoisomerization, while bound to its high-affinity site on human serum albumin, and is an intermediate in the transformation of (ZZ)-bilirubin into (EZ)-cyclobilirubin.

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