Fluorescence properties of Phycocyanin and Phycocyanin-human serum albumin complex

• Published in: Spectrochimica acta. Part A, Molecular and biomolecular spectroscopy Vol. 239; p. 118468
• Main Authors: Seyedi, S., Parvin, P., Jafargholi, A., Jelvani, S., Shahabi, M., Shahbazi, M., Mohammadimatin, P., Moafi, A.
• Format: Journal Article
• Language: English
• Published: England Elsevier B.V 05.10.2020
• Subjects: Binding Sites; Fluorescence properties; Human serum albumin (HSA); Humans; Laser induced fluorescence (LIF); Phycocyanin; Phycocyanin (PC); Protein Binding; Quenching coefficient; Serum Albumin - metabolism; Serum Albumin, Human; Spectrometry, Fluorescence; Stern-Volmer formalism; Stern-Volmer formalism; Quenching coefficient; Fluorescence properties; Laser induced fluorescence (LIF); Human serum albumin (HSA); Phycocyanin (PC)
• ISSN: 1386-1425; 1873-3557
• DOI: 10.1016/j.saa.2020.118468

In this work, the fluorescence properties of Phycocyanin (PC) and the corresponding quenching effects are investigated in attendance of human serum albumin (HSA). At first, PC is excited at 532 nm using CW SHG Nd:YAG laser, then the emission wavelength, Stokes shift, quantum yield, extinction constant and self-quenching coefficient are obtained based on the modified Beer-Lambert equation. It is shown that a notable red shift appears in terms of PC concentration. According to the fluorescence spectra, the addition of HSA in PC solution leads to a significant reduction in the fluorescence signal via quenching events, however a lucid blue shift takes place in the same time. Stern-Volmer formalism is used to determine the quenching constant (KS), the number of binding sites (n) between PC and HSA as well as the association constant Ka for the purpose of facile transportation to the target in the context of drug delivery. Eventually, temperature dependent coefficients and corresponding spectral shifts are investigated over a wide range of temperatures at a couple of distinct PC concentrations to attest the dominant static quenching takes place. The rate of conjugate formations elevates at low temperatures leading to a certain blue shift. Furthermore, large KS is measured in the course of signal reduction, particularly at low PC populations. In fact, PC conjugation to HSA is essential interaction to enhance chemo drug transportation. Here, at the body temperature, the quenching coefficient decreases to facilitate the drug release. Moreover, the spectral shift of fluorescence emission can be useful for simultaneous monitoring and drug delivery treatment. [Display omitted] •Fluorescence signal emission and spectral red shift of PCB versus PC concentration•Assessment of static quenching mechanism via Stern-Volmer formalism•Correlation between spectral blue shift and the quenching coefficient in HSA-PC conjugates over a wide range of temperature•Potential of HSA-PC conjugate as a carrier/antioxidant for drug delivery and cancer therapy