Study on the interaction between 21-(Ph-NN)-NCTPP and bovine serum albumin by spectroscopic techniques

• Published in: Spectrochimica acta. Part A, Molecular and biomolecular spectroscopy Vol. 142; pp. 260 - 265
• Main Authors: Yu, Xianyong, Jiang, Bingfei, Liao, Zhixi, Li, Xiaofang
• Format: Journal Article
• Language: English
• Published: England Elsevier B.V 05.05.2015
• Subjects: 21-(Ph-N[dbnd]N)-NCTPP; Animals; Binding Sites; Bovine serum albumin; Cattle; Energy Transfer; Fluorescence spectroscopy; Hydrophobic and Hydrophilic Interactions; Interaction; Porphyrins - metabolism; Protein Binding; Serum Albumin, Bovine - metabolism; Spectrometry, Fluorescence; Spectrophotometry, Ultraviolet; Thermodynamics; Ultraviolet–visible spectroscopy; Fluorescence spectroscopy; 21-(Ph-NN)-NCTPP; Bovine serum albumin; Interaction; Ultraviolet–visible spectroscopy

[Display omitted] •The interaction between BSA and 21-(ph-NN)-NCTPP was studied.•The fluorescence quenching mechanism was explored.•The binding constants and binding sites were calculated.•Hydrophobic interaction played a major role in the binding process.•High probability of the energy transfer fro...