Spectroscopic analyses on interaction of bovine serum albumin with novel spiro[cyclopropane-pyrrolizin]
- PMID: 25218221
- DOI: 10.1016/j.saa.2014.08.098
Spectroscopic analyses on interaction of bovine serum albumin with novel spiro[cyclopropane-pyrrolizin]
Abstract
The interaction between novel spiro[cyclopropane-pyrrolizin] (NSCP) and bovine serum albumin (BSA) was analyzed by fluorescence and ultraviolet-visible (UV-Vis) spectroscopy at 298 K, 304 K and 310 K under simulative physiological conditions. The results showed that NSCP can effectively quench the intrinsic fluorescence of BSA via static quenching. The binding constants, binding sites of NSCP with BSA were calculated. Hydrogen binds and van der Waals force played a major role in stabilizing the complex and the binding reaction were spontaneous. According to the Förster non-radiation energy transfer theory, the average binding distances between NSCP and BSA were obtained. What is more, the synchronous fluorescence spectra indicated that the conformation of BSA has been changed.
Keywords: Bovine serum albumin; Fluorescence spectroscopy; Interaction; Novel spiro[cyclopropane-pyrrolizin]; Ultraviolet–visible spectroscopy.
Copyright © 2014 Elsevier B.V. All rights reserved.
Similar articles
-
Study on the interaction between novel spiro pyrrolidine and bovine serum albumin by spectroscopic techniques.Spectrochim Acta A Mol Biomol Spectrosc. 2012 Aug;94:23-9. doi: 10.1016/j.saa.2012.03.050. Epub 2012 Mar 29. Spectrochim Acta A Mol Biomol Spectrosc. 2012. PMID: 22503872
-
Spectroscopic studies on the interaction of BSA and 5-spiro-3'-piperidine-2″-spiro-3″-indole-4',2″-diones.Spectrochim Acta A Mol Biomol Spectrosc. 2013 Mar;104:519-26. doi: 10.1016/j.saa.2012.11.095. Epub 2012 Dec 5. Spectrochim Acta A Mol Biomol Spectrosc. 2013. PMID: 23291115
-
The fluorescence spectroscopic study on the interaction between imidazo[2,1-b]thiazole analogues and bovine serum albumin.Spectrochim Acta A Mol Biomol Spectrosc. 2011 Dec;83(1):322-8. doi: 10.1016/j.saa.2011.08.038. Epub 2011 Aug 27. Spectrochim Acta A Mol Biomol Spectrosc. 2011. PMID: 21917505
-
Spectroscopic studies on interaction and sonodynamic damage of metallochlorophyllin (Chl-M (M=Fe, Zn and Cu)) to protein under ultrasonic irradiation.Spectrochim Acta A Mol Biomol Spectrosc. 2011 Sep;79(5):849-57. doi: 10.1016/j.saa.2011.05.085. Epub 2011 Jun 1. Spectrochim Acta A Mol Biomol Spectrosc. 2011. PMID: 21680231 Review.
-
Drug-protein binding: recent advances in methodology: spectroscopic techniques.Ann N Y Acad Sci. 1973 Nov 26;226:44-59. doi: 10.1111/j.1749-6632.1973.tb20467.x. Ann N Y Acad Sci. 1973. PMID: 4129140 Review. No abstract available.
Cited by
-
Binding interaction of phosphorus heterocycles with bovine serum albumin: A biochemical study.J Pharm Anal. 2017 Feb;7(1):19-26. doi: 10.1016/j.jpha.2016.05.009. Epub 2016 Jun 15. J Pharm Anal. 2017. PMID: 29404014 Free PMC article.
-
Interaction of high pressure-stressed soy protein isolate and 5-methyltetrahydrofolate and its impact on the stability of 5-methyltetrahydrofolate.Curr Res Food Sci. 2025 Aug 12;11:101169. doi: 10.1016/j.crfs.2025.101169. eCollection 2025. Curr Res Food Sci. 2025. PMID: 40860686 Free PMC article.
-
Recent Updates on Interaction Studies and Drug Delivery of Antimalarials with Serum Albumin Proteins.Curr Med Chem. 2024;31(25):3925-3953. doi: 10.2174/0929867330666230509121931. Curr Med Chem. 2024. PMID: 37218197 Review.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
