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Interfacial Interactions of a Myoglobin/DOPC Hybrid System at the Air–Water Interface and Its Physicochemical Properties
[Image: see text] In the present study, the intermolecular interactions between a water-insoluble phospholipid (DOPC) and water-soluble protein (myoglobin) and the interaction among themselves were investigated at the air–water interface using the Langmuir and Langmuir–Blodgett techniques. The effec...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American Chemical Society
2023
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10448488/ https://www.ncbi.nlm.nih.gov/pubmed/37636970 http://dx.doi.org/10.1021/acsomega.3c02909 |
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author | Ahmed, Ikbal Das, Nilanjan Islam, A. K. M. Maidul Plaisier, Jasper Rikkert Parisse, Pietro Bal, Jayanta Kumar |
author_facet | Ahmed, Ikbal Das, Nilanjan Islam, A. K. M. Maidul Plaisier, Jasper Rikkert Parisse, Pietro Bal, Jayanta Kumar |
author_sort | Ahmed, Ikbal |
collection | PubMed |
description | [Image: see text] In the present study, the intermolecular interactions between a water-insoluble phospholipid (DOPC) and water-soluble protein (myoglobin) and the interaction among themselves were investigated at the air–water interface using the Langmuir and Langmuir–Blodgett techniques. The effects of changes in physicochemical factors, like pH and temperature, on these interactions were also examined. Surface pressure–molecular area (π–A) isotherms of the DOPC monolayer at the air–water interface, with and without myoglobin (Myo) revealed the evolution of various physical properties, such as elastic, thermodynamic, and hysteric properties, in response to changes in subphase pH and temperature. With the increment of subphase pH from 5 to 7 at a fixed temperature (20 °C), the DOPC isotherm expanded, and the in-plane elasticity (C(S)(–1)) decreased, but no significant presence of hysteresis was encountered in either of the pH values. On the other hand, a diminution of temperature (from 20 to 5 °C) leads to an expansion of monolayers yielding low elasticity and significant hysteresis. The incorporation of Myo molecules within the DOPC monolayer decreased the C(S)(–1) value of the DOPC monolayer. Such a decrement in C(S)(–1) was also encountered while increasing the pH and decreasing the temperature (T) of the subphase in the absence of Myo. Systematic expansion of DOPC isotherm and increased hysteric area with the increase in Myo proportion were observed and the atomic force microscopy (AFM) observations suggested a strong conjugation between Myo and DOPC in the mixed monolayer. The denaturation effect of Myo molecules was studied using AFM at different temperatures. Furthermore, the Myo molecules were found to be most surface active at pH = 7, which is very close to its isoelectric point. These observations come up with the interaction mechanism between biomolecules under dynamically varied conditions. |
format | Online Article Text |
id | pubmed-10448488 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | American Chemical Society |
record_format | MEDLINE/PubMed |
spelling | pubmed-104484882023-08-25 Interfacial Interactions of a Myoglobin/DOPC Hybrid System at the Air–Water Interface and Its Physicochemical Properties Ahmed, Ikbal Das, Nilanjan Islam, A. K. M. Maidul Plaisier, Jasper Rikkert Parisse, Pietro Bal, Jayanta Kumar ACS Omega [Image: see text] In the present study, the intermolecular interactions between a water-insoluble phospholipid (DOPC) and water-soluble protein (myoglobin) and the interaction among themselves were investigated at the air–water interface using the Langmuir and Langmuir–Blodgett techniques. The effects of changes in physicochemical factors, like pH and temperature, on these interactions were also examined. Surface pressure–molecular area (π–A) isotherms of the DOPC monolayer at the air–water interface, with and without myoglobin (Myo) revealed the evolution of various physical properties, such as elastic, thermodynamic, and hysteric properties, in response to changes in subphase pH and temperature. With the increment of subphase pH from 5 to 7 at a fixed temperature (20 °C), the DOPC isotherm expanded, and the in-plane elasticity (C(S)(–1)) decreased, but no significant presence of hysteresis was encountered in either of the pH values. On the other hand, a diminution of temperature (from 20 to 5 °C) leads to an expansion of monolayers yielding low elasticity and significant hysteresis. The incorporation of Myo molecules within the DOPC monolayer decreased the C(S)(–1) value of the DOPC monolayer. Such a decrement in C(S)(–1) was also encountered while increasing the pH and decreasing the temperature (T) of the subphase in the absence of Myo. Systematic expansion of DOPC isotherm and increased hysteric area with the increase in Myo proportion were observed and the atomic force microscopy (AFM) observations suggested a strong conjugation between Myo and DOPC in the mixed monolayer. The denaturation effect of Myo molecules was studied using AFM at different temperatures. Furthermore, the Myo molecules were found to be most surface active at pH = 7, which is very close to its isoelectric point. These observations come up with the interaction mechanism between biomolecules under dynamically varied conditions. American Chemical Society 2023-08-12 /pmc/articles/PMC10448488/ /pubmed/37636970 http://dx.doi.org/10.1021/acsomega.3c02909 Text en © 2023 The Authors. Published by American Chemical Society https://creativecommons.org/licenses/by-nc-nd/4.0/Permits non-commercial access and re-use, provided that author attribution and integrity are maintained; but does not permit creation of adaptations or other derivative works (https://creativecommons.org/licenses/by-nc-nd/4.0/). |
spellingShingle | Ahmed, Ikbal Das, Nilanjan Islam, A. K. M. Maidul Plaisier, Jasper Rikkert Parisse, Pietro Bal, Jayanta Kumar Interfacial Interactions of a Myoglobin/DOPC Hybrid System at the Air–Water Interface and Its Physicochemical Properties |
title | Interfacial Interactions
of a Myoglobin/DOPC Hybrid
System at the Air–Water Interface and Its Physicochemical Properties |
title_full | Interfacial Interactions
of a Myoglobin/DOPC Hybrid
System at the Air–Water Interface and Its Physicochemical Properties |
title_fullStr | Interfacial Interactions
of a Myoglobin/DOPC Hybrid
System at the Air–Water Interface and Its Physicochemical Properties |
title_full_unstemmed | Interfacial Interactions
of a Myoglobin/DOPC Hybrid
System at the Air–Water Interface and Its Physicochemical Properties |
title_short | Interfacial Interactions
of a Myoglobin/DOPC Hybrid
System at the Air–Water Interface and Its Physicochemical Properties |
title_sort | interfacial interactions
of a myoglobin/dopc hybrid
system at the air–water interface and its physicochemical properties |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10448488/ https://www.ncbi.nlm.nih.gov/pubmed/37636970 http://dx.doi.org/10.1021/acsomega.3c02909 |
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