Features of the complex of food additive hesperidin to hemoglobin

Ding, Fei; Sun, Ye; Diao, Jian-Xiong; Li, Xiu-Nan; Yang, Xinling; Sun, Ying; Zhang, Li

doi:10.1016/j.jphotobiol.2011.10.004

Cited by 12 publications

(1 citation statement)

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“…It shows that a band in the near-UV region with a maximum 278 nm, which appears due to phenyl group of tryptophan. The UVvisible spectra of donor was not altered only when excited-state of fluorescent molecule influenced by quenchers for dynamic quenching; but for static quenching a complex is appeared between fluorophore and quencher [20]. The absorption spectrum of Trp was changed due to formation of ground state complex.…”

Section: Uv-visible Absorption Spectral Studiesmentioning

confidence: 95%

Spectroscopic insights on the interaction between 4-(3,4 dimethoxyphenyl)-6-hydroxy-2- methylpyrimidine-5-carbonitrile and tryptophan.

Patil¹,

Undre²,

Salunkhe³

et al. 2019

JCPR

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The interaction between 4-(3,4-dimethoxyphenyl)-6-hydroxy-2-methylpyrimidine-5-carbonitrile (DMPHMPC) and tryptophan (Trp) has been explored by fluorescence and Uv-visible studies. The formation of DMPHMPC-Trp complex leads to the fluorescence quenching of Trp was induced by DMPHMPC and evaluated by spectrofluorimetry. The fluorescence mechanism of Trp due to DMPHMPC is static in nature as analyzed by temperature effect study. Stern-Volmer quenching constants (Ksv) between DMPHMPC and Trp at three different temperatures 303, 308 and 313 K were obtained to be 9.12 x 10-3 , 4.07 x 10-3 and 1.63 x 10-3 L mol-1 , respectively which detected that the binding mechanism between DMPHMPC and Trp is predominantly static in nature. The calculated binding constants were 3.96 x 10-4 , 3.61 x 10-4 and 2.85 x 10-4 L mol-1 , respectively. The numbers of binding sites were 1.01, 0.92 and 0.91. Enthalpy change (ΔH) and Entropy change (ΔS) has positive value which indicates that hydrophobic interactions played a major role in the binding mechanism. Synchronous fluorescence suggesting that DMPHMPC bonded to Trp and placed in the close vicinity of Trp. Whereas the binding distance (r) between DMPHMPC and Trp was obtained to be 4.46 nm by Forster's theory of nonradiative energy transfer .

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Section: Uv-visible Absorption Spectral Studiesmentioning

confidence: 95%