Interaction Between Fluorinated Amphiphilic Copolymer P(HFMA)-g-P(SPEG) and BSA

Abstract

A novel fluorinated amphiphilic copolymer P(HFMA)-g-P(SPEG) was synthesized. The interactions between P(HFMA)-g-P(SPEG) and bovine serum albumin (BSA) were studied by synchronous fluorescence and intrinsic fluorescence spectroscopy. It was concluded through synchronous fluorescence that P(HFMA)-g-P(SPEG) mainly bound to tryptophan residues of BSA. Intrinsic fluorescence results revealed that BSA and P(HFMA)-g-P(SPEG) had strong interactions. The mechanism of quenching belonged to dynamic quenching and the main sort of binding force was hydrophobic force. The hydrophobic interaction between P(HFMA)-g-P(SPEG) and BSA was conformed by micropolarity and TEM photographs.

Keywords:

• BSA
• fluorescence
• fluorinated amphiphilic copolymer
• hydrophobic interaction

Acknowledgments

This work was supported by the Hong Kong Research Grants Council (RGC) General Research Funds (GRF) No. CityU 112306.

Notes

R is the linear quotiety.