FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W4221119476> ?p ?o ?g. }

• W4221119476 endingPage "119042" @default.
• W4221119476 startingPage "119042" @default.
• W4221119476 abstract "We examined the inducement of an interaction between two carrier proteins, human serum albumin (HSA) and human holo transferrin (HTF) within the presence of cyanidinin the form of binary and ternary systems, which was conducted by different spectroscopic, isothermal titration calorimetric (ITC), and molecular dynamics simulation techniques. The results of fluorescence spectroscopy verified the occurrence of this interaction by displaying the regular quenching of emission spectra of proteins as single and complex forms by cyanidin. Moreover, fluorescence emission suggested that, HSA-cyanidin, HTF-cyanidin and (HSA-HTF) cyanidin complexes follows an static mechanism with the binding constants of 8.81 × 104, 3.40 × 104, and 7.10 × 104 M−1, respectively, which were strongly reflected to moderate the affinity of cyanidin to both single and complex forms of proteins. The measured thermodynamic parameters obtained by ITC, determined the necessity of electrostatic forces for binding of cyanidin to HSA and HTF. Besides, obtaining a negative ΔG0 is indicative of spontaneous mode of binding process in both conditions. The different values of thermodynamic parameters of cyanidin binding to the forms of HSA, HTF and HSA-HTF complex clearly proved the similarity in the type of interaction forces between cyanidin and proteins as single and complex forms with various values. The observed changes in synchronous fluorescence results were related to the micro-environment properties of Tyr and Trp residues. The induced alternations in the secondary construction of both proteins were confirmed through the outcomes of quantitative analysis performed by circular dichroism spectroscopy (CD) techniques. FRET theory was exerted to calculate, the existing distance across the donor and acceptor, which were reported to be 1.85 nm, 1.97 nm, and 1.91 nm for the cases of HSA-cyanidin, HTF-cyanidin and (HSA-HTF) cyanidin complexes, respectively. Molecular displacement and protein–ligand docking simulations confirmed the binding of cyanidin to HSA and HTF through the binary and ternary systems." @default.
• W4221119476 created "2022-04-03" @default.
• W4221119476 creator A5016964015 @default.
• W4221119476 creator A5024459995 @default.
• W4221119476 creator A5036086680 @default.
• W4221119476 creator A5036115917 @default.
• W4221119476 creator A5044310674 @default.
• W4221119476 creator A5062696367 @default.
• W4221119476 creator A5069960428 @default.
• W4221119476 creator A5073517218 @default.
• W4221119476 creator A5079343839 @default.
• W4221119476 date "2022-06-01" @default.
• W4221119476 modified "2023-10-06" @default.
• W4221119476 title "Novel perspective into the interaction behavior study of the cyanidin with human serum albumin-holo transferrin complex: Spectroscopic, calorimetric and molecular modeling approaches" @default.
• W4221119476 cites W1511599028 @default.
• W4221119476 cites W1969042039 @default.
• W4221119476 cites W1971942980 @default.
• W4221119476 cites W2005947510 @default.
• W4221119476 cites W2018421404 @default.
• W4221119476 cites W2018503874 @default.
• W4221119476 cites W2019047431 @default.
• W4221119476 cites W2029967497 @default.
• W4221119476 cites W2034555311 @default.
• W4221119476 cites W2036644638 @default.
• W4221119476 cites W2045534377 @default.
• W4221119476 cites W2051754303 @default.
• W4221119476 cites W2052881431 @default.
• W4221119476 cites W2070213522 @default.
• W4221119476 cites W2080537375 @default.
• W4221119476 cites W2087017753 @default.
• W4221119476 cites W2102557954 @default.
• W4221119476 cites W2144852755 @default.
• W4221119476 cites W2154186092 @default.
• W4221119476 cites W2264742377 @default.
• W4221119476 cites W2316740535 @default.
• W4221119476 cites W2434769785 @default.
• W4221119476 cites W2488221317 @default.
• W4221119476 cites W2500915768 @default.
• W4221119476 cites W2529659446 @default.
• W4221119476 cites W2604337791 @default.
• W4221119476 cites W2606537295 @default.
• W4221119476 cites W2619671559 @default.
• W4221119476 cites W2620897937 @default.
• W4221119476 cites W2738793161 @default.
• W4221119476 cites W2760849264 @default.
• W4221119476 cites W2768070124 @default.
• W4221119476 cites W2787446985 @default.
• W4221119476 cites W2789885929 @default.
• W4221119476 cites W2800668305 @default.
• W4221119476 cites W2805238516 @default.
• W4221119476 cites W2896931964 @default.
• W4221119476 cites W2898335604 @default.
• W4221119476 cites W2901516736 @default.
• W4221119476 cites W2902888828 @default.
• W4221119476 cites W2903973384 @default.
• W4221119476 cites W2908942568 @default.
• W4221119476 cites W2912856690 @default.
• W4221119476 cites W2914373961 @default.
• W4221119476 cites W2915030754 @default.
• W4221119476 cites W2924317848 @default.
• W4221119476 cites W2938235822 @default.
• W4221119476 cites W2943019002 @default.
• W4221119476 cites W2946313636 @default.
• W4221119476 cites W2954287414 @default.
• W4221119476 cites W2954783091 @default.
• W4221119476 cites W2963716106 @default.
• W4221119476 cites W2964381777 @default.
• W4221119476 cites W2964381891 @default.
• W4221119476 cites W2968692331 @default.
• W4221119476 cites W2980508386 @default.
• W4221119476 cites W2980789286 @default.
• W4221119476 cites W2985743431 @default.
• W4221119476 cites W3005765771 @default.
• W4221119476 cites W3006385966 @default.
• W4221119476 cites W3009237862 @default.
• W4221119476 cites W3014472662 @default.
• W4221119476 cites W3080279151 @default.
• W4221119476 cites W3108283031 @default.
• W4221119476 cites W3136881362 @default.
• W4221119476 cites W3170217324 @default.
• W4221119476 cites W3205107265 @default.
• W4221119476 cites W3207737431 @default.
• W4221119476 cites W4200389293 @default.
• W4221119476 cites W4205538970 @default.
• W4221119476 cites W2953763689 @default.
• W4221119476 doi "https://doi.org/10.1016/j.molliq.2022.119042" @default.
• W4221119476 hasPublicationYear "2022" @default.
• W4221119476 type Work @default.
• W4221119476 citedByCount "82" @default.
• W4221119476 countsByYear W42211194762022 @default.
• W4221119476 countsByYear W42211194762023 @default.
• W4221119476 crossrefType "journal-article" @default.
• W4221119476 hasAuthorship W4221119476A5016964015 @default.
• W4221119476 hasAuthorship W4221119476A5024459995 @default.
• W4221119476 hasAuthorship W4221119476A5036086680 @default.
• W4221119476 hasAuthorship W4221119476A5036115917 @default.
• W4221119476 hasAuthorship W4221119476A5044310674 @default.
• W4221119476 hasAuthorship W4221119476A5062696367 @default.

• next