Thermal investigation of montmorillonite/BSA by fourier transform infrared spectroscopy measurements
This paper reports the analysis of the intramolecular OH stretching band obtained by Fourier Transform Infrared (FTIR) spectroscopy measurements. In order to characterize the effect of montmorillonite on the properties of Bovine Serum Albumin (BSA) the two-state model is adopted for the analysis of...
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AIMS Press
2020-12-01
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author | Maria Teresa Caccamo Giuseppe Mavilia Letterio Mavilia Pietro Calandra Domenico Lombardo Salvatore Magazù |
author_facet | Maria Teresa Caccamo Giuseppe Mavilia Letterio Mavilia Pietro Calandra Domenico Lombardo Salvatore Magazù |
author_sort | Maria Teresa Caccamo |
collection | DOAJ |
description | This paper reports the analysis of the intramolecular OH stretching band obtained by Fourier Transform Infrared (FTIR) spectroscopy measurements. In order to characterize the effect of montmorillonite on the properties of Bovine Serum Albumin (BSA) the two-state model is adopted for the analysis of the OH stretching band. We assume that the OH stretching can be divided into two different states of inter-molecular bonding. The results of this experimental work confirm that the montmorillonite leads to a stabilization of the BSA structure. Also, the analysis of the spectra temperature dependence shows a montmorillonite-induced higher thermal stability of the BSA in respect to pristine BSA. Thus, this paper highlights the effectiveness of montmorillonite as thermal bio-protector. A FTIR analysis was carried out to investigate the interaction of Montmorillonite with BSA. Two different approaches, i.e. Spectral Distance and Wavelet analyses, constitute two effective and innovative approaches for the characterization of the thermal properties of pristine BSA and of BSA in the presence of Montmorillonite. The results allowed us to consider as BSA in the presence of Montmorillonite has a lower spectral sensitivity when the temperature changes and, therefore, the role of Montmorillonite as a thermal bio-protector is motivated. |
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spelling | doaj.art-010796a7bc334fa1ad3e22f1798099962022-12-22T02:06:55ZengAIMS PressAIMS Biophysics2377-90982020-12-017443645110.3934/biophy.2020030Thermal investigation of montmorillonite/BSA by fourier transform infrared spectroscopy measurementsMaria Teresa Caccamo0Giuseppe Mavilia1Letterio Mavilia2Pietro Calandra3Domenico Lombardo 4Salvatore Magazù51. Dipartimento di Scienze Matematiche e Informatiche, Scienze Fisiche e Scienze della Terra, Università di Messina, Viale Ferdinando Stagno D'Alcontres n 31, S. Agata, 98166 Messina, Italy1. Dipartimento di Scienze Matematiche e Informatiche, Scienze Fisiche e Scienze della Terra, Università di Messina, Viale Ferdinando Stagno D'Alcontres n 31, S. Agata, 98166 Messina, Italy2. Dipartimento di Patrimonio, Architettura e Urbanistica; Università Mediterranea di Reggio Calabria, (PAU), Via Melissari, I-89124 Reggio Calabria, Italy3. Consiglio Nazionale delle Ricerche, Istituto per lo Studio Materiali Nanostrutturati, Via Salaria Km 29,300 00015 Monterotondo Stazione (Roma), Italy4. CNR–IPCF, Istituto per i Processi Chimico Fisici – (Sez. Messina) Viale F. Stagno D'Alcontres, 37. I-98158, Messina, Italy1. Dipartimento di Scienze Matematiche e Informatiche, Scienze Fisiche e Scienze della Terra, Università di Messina, Viale Ferdinando Stagno D'Alcontres n 31, S. Agata, 98166 Messina, ItalyThis paper reports the analysis of the intramolecular OH stretching band obtained by Fourier Transform Infrared (FTIR) spectroscopy measurements. In order to characterize the effect of montmorillonite on the properties of Bovine Serum Albumin (BSA) the two-state model is adopted for the analysis of the OH stretching band. We assume that the OH stretching can be divided into two different states of inter-molecular bonding. The results of this experimental work confirm that the montmorillonite leads to a stabilization of the BSA structure. Also, the analysis of the spectra temperature dependence shows a montmorillonite-induced higher thermal stability of the BSA in respect to pristine BSA. Thus, this paper highlights the effectiveness of montmorillonite as thermal bio-protector. A FTIR analysis was carried out to investigate the interaction of Montmorillonite with BSA. Two different approaches, i.e. Spectral Distance and Wavelet analyses, constitute two effective and innovative approaches for the characterization of the thermal properties of pristine BSA and of BSA in the presence of Montmorillonite. The results allowed us to consider as BSA in the presence of Montmorillonite has a lower spectral sensitivity when the temperature changes and, therefore, the role of Montmorillonite as a thermal bio-protector is motivated.http://www.aimspress.com/article/doi/10.3934/biophy.2020030?viewType=HTMLbovine sserum albuminmontmorillonitefourier transform infrared spectroscopy |
spellingShingle | Maria Teresa Caccamo Giuseppe Mavilia Letterio Mavilia Pietro Calandra Domenico Lombardo Salvatore Magazù Thermal investigation of montmorillonite/BSA by fourier transform infrared spectroscopy measurements AIMS Biophysics bovine sserum albumin montmorillonite fourier transform infrared spectroscopy |
title | Thermal investigation of montmorillonite/BSA by fourier transform infrared spectroscopy measurements |
title_full | Thermal investigation of montmorillonite/BSA by fourier transform infrared spectroscopy measurements |
title_fullStr | Thermal investigation of montmorillonite/BSA by fourier transform infrared spectroscopy measurements |
title_full_unstemmed | Thermal investigation of montmorillonite/BSA by fourier transform infrared spectroscopy measurements |
title_short | Thermal investigation of montmorillonite/BSA by fourier transform infrared spectroscopy measurements |
title_sort | thermal investigation of montmorillonite bsa by fourier transform infrared spectroscopy measurements |
topic | bovine sserum albumin montmorillonite fourier transform infrared spectroscopy |
url | http://www.aimspress.com/article/doi/10.3934/biophy.2020030?viewType=HTML |
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