{"title":"Spectroscopic characterization of triazine based covalent organic framework tempted changes in the structure of hemoglobin","authors":"Nitanshu Dhama , Karan Chaudhary , Rohit Yadav , Dhanraj T. Masram","doi":"10.1016/j.saa.2024.125320","DOIUrl":null,"url":null,"abstract":"<div><div>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 T<sub>m</sub> 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.</div></div>","PeriodicalId":433,"journal":{"name":"Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy","volume":"327 ","pages":"Article 125320"},"PeriodicalIF":4.3000,"publicationDate":"2024-10-22","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy","FirstCategoryId":"92","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/S1386142524014860","RegionNum":2,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q1","JCRName":"SPECTROSCOPY","Score":null,"Total":0}
引用次数: 0
Abstract
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.
期刊介绍:
Spectrochimica Acta, Part A: Molecular and Biomolecular Spectroscopy (SAA) is an interdisciplinary journal which spans from basic to applied aspects of optical spectroscopy in chemistry, medicine, biology, and materials science.
The journal publishes original scientific papers that feature high-quality spectroscopic data and analysis. From the broad range of optical spectroscopies, the emphasis is on electronic, vibrational or rotational spectra of molecules, rather than on spectroscopy based on magnetic moments.
Criteria for publication in SAA are novelty, uniqueness, and outstanding quality. Routine applications of spectroscopic techniques and computational methods are not appropriate.
Topics of particular interest of Spectrochimica Acta Part A include, but are not limited to:
Spectroscopy and dynamics of bioanalytical, biomedical, environmental, and atmospheric sciences,
Novel experimental techniques or instrumentation for molecular spectroscopy,
Novel theoretical and computational methods,
Novel applications in photochemistry and photobiology,
Novel interpretational approaches as well as advances in data analysis based on electronic or vibrational spectroscopy.