Fluorescence Study on the Interaction of Human-Like Collagen and Copper(II)

Abstract

Fluorescence spectroscopy and UV-VIS absorption spectroscopy were employed to analyze the binding of Cu²⁺ to human-like collagen (HLC) with Cu²⁺ concentrations from 0 to 1.0 × 10^-4 mol L^-1 at 273 and 298 K. The fluorescence titration results indicated that Cu²⁺ quenched the fluorescence intensity of human-like collagen and the quenching mechanism should belong to both dynamic and static quenching according to the Stern-Volmer equation. The binding constants and the corresponding thermodynamic parameters at different temperatures were calculated, which showed that hydrophobic interactions were the main binding force. The conclusion that Cu²⁺ could bind to human-like collagen was clarified by all these experimental results and theoretical data, and it could be a useful guideline for further study of human-like collagen-Cu complex.