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Unfolding and Refolding of Protein by a Combination of Ionic and Nonionic Surfactants

[Image: see text] The interaction of protein and surfactant yields protein–surfactant complexes which have a wide range of applications in the cosmetics, foods, and pharmaceutical industries among others. Ionic and nonionic surfactants are known to interact differently with the protein. The interpla...

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Autores principales: Saha, Debasish, Ray, Debes, Kohlbrecher, Joachim, Aswal, Vinod Kumar
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Chemical Society 2018
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6645170/
https://www.ncbi.nlm.nih.gov/pubmed/31458962
http://dx.doi.org/10.1021/acsomega.8b00630
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author Saha, Debasish
Ray, Debes
Kohlbrecher, Joachim
Aswal, Vinod Kumar
author_facet Saha, Debasish
Ray, Debes
Kohlbrecher, Joachim
Aswal, Vinod Kumar
author_sort Saha, Debasish
collection PubMed
description [Image: see text] The interaction of protein and surfactant yields protein–surfactant complexes which have a wide range of applications in the cosmetics, foods, and pharmaceutical industries among others. Ionic and nonionic surfactants are known to interact differently with the protein. The interplay of electrostatic and hydrophobic interactions governs the resultant structure of protein–surfactant complexes. The present study enlightens the paramount role of the hydrophobic interaction, tuned by the hydrophobic tail length of ionic surfactants, in the unfolding of anionic bovine serum albumin (BSA) protein. The unfolding of BSA in the presence of four different tail-length cationic surfactants, that is, C10TAB, C12TAB, C14TAB, and C16TAB, has been investigated by small-angle neutron scattering and dynamic light scattering. All cationic surfactants unfold the protein at a certain concentration range. The propensity of protein unfolding increases with increasing the hydrophobic tail length. The denatured structure of BSA upon addition of cationic surfactants is characterized by the random flight model representing a beads-on-a-string chain-like complex. The unfolded protein binds the surfactant micelles in the protein–surfactant cluster. The micelles get elongated with the increasing concentration of cationic surfactants, whereas the number of micelles per cluster is decreased. In the final stage, the protein–surfactant cluster merges to one large micelle with unfolded protein wrapping the micelle surface. The pathway of protein unfolding is described in terms of the changes in the micellar size, the number of micelles formed per cluster, the separation between the micelles in the cluster, the aggregation number of micelles, and the number of proteins per cluster. The protein–surfactant interaction is further examined in the presence of a nonionic surfactant, that is, C12E10. The nonionic surfactant significantly suppresses the interaction of BSA protein with ionic surfactants by forming mixed micelles. As a result of the mixed micelles formation by ionic–nonionic surfactants, the ionic surfactant moves out from the unfolded BSA protein, and this enables the protein to refold back to its native structure. The propensity of mixed micelle-driven refolding of proteins is significantly changed with changing the tail length of the ionic surfactant.
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spelling pubmed-66451702019-08-27 Unfolding and Refolding of Protein by a Combination of Ionic and Nonionic Surfactants Saha, Debasish Ray, Debes Kohlbrecher, Joachim Aswal, Vinod Kumar ACS Omega [Image: see text] The interaction of protein and surfactant yields protein–surfactant complexes which have a wide range of applications in the cosmetics, foods, and pharmaceutical industries among others. Ionic and nonionic surfactants are known to interact differently with the protein. The interplay of electrostatic and hydrophobic interactions governs the resultant structure of protein–surfactant complexes. The present study enlightens the paramount role of the hydrophobic interaction, tuned by the hydrophobic tail length of ionic surfactants, in the unfolding of anionic bovine serum albumin (BSA) protein. The unfolding of BSA in the presence of four different tail-length cationic surfactants, that is, C10TAB, C12TAB, C14TAB, and C16TAB, has been investigated by small-angle neutron scattering and dynamic light scattering. All cationic surfactants unfold the protein at a certain concentration range. The propensity of protein unfolding increases with increasing the hydrophobic tail length. The denatured structure of BSA upon addition of cationic surfactants is characterized by the random flight model representing a beads-on-a-string chain-like complex. The unfolded protein binds the surfactant micelles in the protein–surfactant cluster. The micelles get elongated with the increasing concentration of cationic surfactants, whereas the number of micelles per cluster is decreased. In the final stage, the protein–surfactant cluster merges to one large micelle with unfolded protein wrapping the micelle surface. The pathway of protein unfolding is described in terms of the changes in the micellar size, the number of micelles formed per cluster, the separation between the micelles in the cluster, the aggregation number of micelles, and the number of proteins per cluster. The protein–surfactant interaction is further examined in the presence of a nonionic surfactant, that is, C12E10. The nonionic surfactant significantly suppresses the interaction of BSA protein with ionic surfactants by forming mixed micelles. As a result of the mixed micelles formation by ionic–nonionic surfactants, the ionic surfactant moves out from the unfolded BSA protein, and this enables the protein to refold back to its native structure. The propensity of mixed micelle-driven refolding of proteins is significantly changed with changing the tail length of the ionic surfactant. American Chemical Society 2018-07-25 /pmc/articles/PMC6645170/ /pubmed/31458962 http://dx.doi.org/10.1021/acsomega.8b00630 Text en Copyright © 2018 American Chemical Society This is an open access article published under an ACS AuthorChoice License (http://pubs.acs.org/page/policy/authorchoice_termsofuse.html) , which permits copying and redistribution of the article or any adaptations for non-commercial purposes.
spellingShingle Saha, Debasish
Ray, Debes
Kohlbrecher, Joachim
Aswal, Vinod Kumar
Unfolding and Refolding of Protein by a Combination of Ionic and Nonionic Surfactants
title Unfolding and Refolding of Protein by a Combination of Ionic and Nonionic Surfactants
title_full Unfolding and Refolding of Protein by a Combination of Ionic and Nonionic Surfactants
title_fullStr Unfolding and Refolding of Protein by a Combination of Ionic and Nonionic Surfactants
title_full_unstemmed Unfolding and Refolding of Protein by a Combination of Ionic and Nonionic Surfactants
title_short Unfolding and Refolding of Protein by a Combination of Ionic and Nonionic Surfactants
title_sort unfolding and refolding of protein by a combination of ionic and nonionic surfactants
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6645170/
https://www.ncbi.nlm.nih.gov/pubmed/31458962
http://dx.doi.org/10.1021/acsomega.8b00630
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