Delicate Analysis of Interacting Proteins and Their Assemblies by Flow Field-Flow Fractionation Techniques
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arXiv
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| Format: | Preprint |
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2024
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| _version_ | 1866916328265220096 |
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| author | Urbes, Aurélien Morel, Marie-Hélène Ramos, Laurence Violleau, Frédéric Banc, Amélie |
| author_facet | Urbes, Aurélien Morel, Marie-Hélène Ramos, Laurence Violleau, Frédéric Banc, Amélie |
| contents | We study the efficiency of several Asymmetrical Flow Field-Flow Fractionation (AF4) techniques to investigate the self-associating wheat gluten proteins. We compare the use of a denaturing buffer including sodium dodecyl sulfate (SDS) and a mild chaotropic solvent, water/ethanol, as eluent, on a model gluten sample. Through a thorough analysis of the data obtained from coupled light scattering detectors, and with the identification of molecular composition of the eluted protein, we evidence co-elution events in several conditions. We show that the focus step used in conventional AF4 with the SDS buffer leads to the formation of aggregates that co-elute with monomeric proteins. By contrast, a frit-inlet device enables the fractionation of individual wheat proteins in the SDS buffer. Interestingly conventional AF4, using water/ethanol as eluent, is an effective method for fractionating gluten proteins and their complex dynamic assemblies which involve weak forces and are composed of both monomeric and polymeric proteins. |
| format | Preprint |
| id |
arxiv_https___arxiv_org_abs_2407_12368 |
| institution | arXiv |
| publishDate | 2024 |
| record_format | arxiv |
| spellingShingle | Delicate Analysis of Interacting Proteins and Their Assemblies by Flow Field-Flow Fractionation Techniques Urbes, Aurélien Morel, Marie-Hélène Ramos, Laurence Violleau, Frédéric Banc, Amélie Soft Condensed Matter Chemical Physics We study the efficiency of several Asymmetrical Flow Field-Flow Fractionation (AF4) techniques to investigate the self-associating wheat gluten proteins. We compare the use of a denaturing buffer including sodium dodecyl sulfate (SDS) and a mild chaotropic solvent, water/ethanol, as eluent, on a model gluten sample. Through a thorough analysis of the data obtained from coupled light scattering detectors, and with the identification of molecular composition of the eluted protein, we evidence co-elution events in several conditions. We show that the focus step used in conventional AF4 with the SDS buffer leads to the formation of aggregates that co-elute with monomeric proteins. By contrast, a frit-inlet device enables the fractionation of individual wheat proteins in the SDS buffer. Interestingly conventional AF4, using water/ethanol as eluent, is an effective method for fractionating gluten proteins and their complex dynamic assemblies which involve weak forces and are composed of both monomeric and polymeric proteins. |
| title | Delicate Analysis of Interacting Proteins and Their Assemblies by Flow Field-Flow Fractionation Techniques |
| topic | Soft Condensed Matter Chemical Physics |
| url | https://arxiv.org/abs/2407.12368 |