2010
DOI: 10.1021/jp907576r
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The Interaction of 5-(Alkoxy)naphthalen-1-amine with Bovine Serum Albumin and Its Effect on the Conformation of Protein

Abstract: The effects of binding and conformational changes induced by the neutral amphiphilic ligand [5-(alkoxy)naphthalen-1-amine] with different alkyl chain lengths on bovine serum albumin (BSA) have been studied using UV-visible and fluorescence spectroscopic methods. The BSA fluorescence exhibits appreciable bathochromic shift along with a reduction in fluorescence intensity and fluorescence lifetime upon binding with ligands. Ligand quenches the fluorescence of BSA in a concentration-dependent manner and deviates … Show more

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Cited by 151 publications
(93 citation statements)
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“…Therefore, it is unlikely that the conformation of HSA will be changed with the level of DMSO used in this study. 97 Milipore water was used in the preparation of buffer solution.…”
Section: Hsa Binding Experimentsmentioning
confidence: 99%
“…Therefore, it is unlikely that the conformation of HSA will be changed with the level of DMSO used in this study. 97 Milipore water was used in the preparation of buffer solution.…”
Section: Hsa Binding Experimentsmentioning
confidence: 99%
“…The fluorescence intensities of these residues decrease in the following order: Trp>Tyr>Phe [30]. Each BSA molecule has two Trp residues, one of which is located at the bottom of the hydrophobic pocket in domain II (Trp-212), while the other is in domain I (Trp-134) on the surface of the molecule [31][32][33]. Because the excited-state dipole moment of Trp is relatively large, the emission energy is highly sensitive to the polarity of the environment.…”
Section: Analysis Of the Aunps-bsa Interactionsmentioning
confidence: 99%
“…Conformational changes in BSA may disturb the microenvironment around the Trp residues and thus influence the fluorescence emission. Therefore, the Trp fluorescence is widely used to monitor conformational changes in proteins [31,34].…”
Section: Analysis Of the Aunps-bsa Interactionsmentioning
confidence: 99%
“…The Gemini amphiphiles has possessed more interaction with BSA, as explained on the basis of higher value of K sv, as compared to single amphiphiles. The synchronous spectra and UV spectra of amphiphiles also show that the unfolding of proteins is mainly due to the interaction between amphiphiles and Trp residues of BSA [32]. TEM studies revealed that the mechanism of binding of single chain amphiphiles is different from that of Gemini amphiphiles.…”
Section: Resultsmentioning
confidence: 97%