Spectroscopic characterization of triazine based covalent organic framework tempted changes in the structure of hemoglobin

[Display omitted] •Spectroscopic characterization for change in Hb structure due to TATF-COF.•Spectroscopy revealed a slight alteration in Hb structure due to conjugation.•Electron microscopy, DLS and zeta displayed formation of Hb-TATF-COF conjugate.•TATF-COF found compatible with Hb as Hb native structure was well-preserved.•Integration of biology and framework materials for advanced bioconjugates. The present study aims to understand changes in the Hemoglobin (Hb) structure in the presence of a triazine based covalent organic framework (COF) through spectroscopic characterization. Covalent Organic Frameworks (COFs) due to their unique properties have been utilized in diverse fields including bio-applications. Utilization of COFs for conjugate formation with proteins will lead to the integration of biology and framework materials that can help in the development of bioconjugates for advanced bio-based applications such as diagnostics, therapeutics, and bioengineering. However, vital is to have a fundamental understanding of protein conformation in protein-COF conjugate. Herein, a triazine based COF has been synthesized via solvothermal method, termed TATF-COF which has been utilized for the formation of a conjugate with hemoglobin (Hb). Thereafter, studies have been performed to understand Hb structure in the presence of TATF-COF. Results from UV–vis, Fluorescence, and UV-CD spectroscopy studies revealed that in the presence of TATF-COF, there was a slight alteration in the Hb structure due to binding interactions between them and conjugate formation. Moreover, micrographs obtained from electron microscopy displayed formation of conjugate between Hb and TATF-COF result of binding interactions. DLS and zeta potential results also revealed conjugate formation due to binding interactions between TATF-COF and Hb. Thermal stability of Hb was also maintained as TATF-COF had insignificant effect on the Tm value of Hb. Overall, there was a slight alternation in the Hb native conformation due to binding interactions, however, TATF-COF was compatible with Hb as the protein’s native structure was well-preserved.