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Frictional behaviour of plant proteins in soft contacts: unveiling nanoscale mechanisms
Despite the significance of nanotribology in the design of functional biomaterials, little is known about nanoscale friction in the presence of protein-coated soft contact surfaces. Here, we report a detailed investigation of frictional behaviour of sustainable plant proteins at the nanoscale for th...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
RSC
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9926882/ https://www.ncbi.nlm.nih.gov/pubmed/36798497 http://dx.doi.org/10.1039/d2na00696k |
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author | Liamas, Evangelos Connell, Simon D. Sarkar, Anwesha |
author_facet | Liamas, Evangelos Connell, Simon D. Sarkar, Anwesha |
author_sort | Liamas, Evangelos |
collection | PubMed |
description | Despite the significance of nanotribology in the design of functional biomaterials, little is known about nanoscale friction in the presence of protein-coated soft contact surfaces. Here, we report a detailed investigation of frictional behaviour of sustainable plant proteins at the nanoscale for the first time, using deformable bio-relevant surfaces that achieve biologically relevant contact pressures. A combination of atomic force microscopy, quartz crystal microbalance with dissipation monitoring, and friction force microscopy with soft polydimethylsiloxane (PDMS, 150 kPa) surfaces was employed to elucidate the frictional properties of model plant proteins, i.e. lupine, pea, and potato proteins at the nanoscale while systematically varying the pH and ionic strength. Interactions of these plant proteins with purified mucins were also probed. We provide the much-needed direct experimental evidence that the main factor dictating the frictional properties of plant proteins is their affinity towards the surface, followed by the degree of protein film hydration. Proteins with high surface affinity, such as pea and potato protein, have better lubricating performance than lupine at the nanoscale. Other minor factors that drive lubrication are surface interactions between sliding bodies, especially at low load, whilst jamming of the contact area caused by larger protein aggregates increases friction. Novel findings reveal that interactions between plant proteins and mucins lead to superior lubricating properties, by combining high surface affinity from the plant proteins and high hydration by mucins. We anticipate that fundamental understanding gained from this work will set the stage for the design of a plethora of sustainable biomaterials and food with optimum nanolubrication performance. |
format | Online Article Text |
id | pubmed-9926882 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | RSC |
record_format | MEDLINE/PubMed |
spelling | pubmed-99268822023-02-15 Frictional behaviour of plant proteins in soft contacts: unveiling nanoscale mechanisms Liamas, Evangelos Connell, Simon D. Sarkar, Anwesha Nanoscale Adv Chemistry Despite the significance of nanotribology in the design of functional biomaterials, little is known about nanoscale friction in the presence of protein-coated soft contact surfaces. Here, we report a detailed investigation of frictional behaviour of sustainable plant proteins at the nanoscale for the first time, using deformable bio-relevant surfaces that achieve biologically relevant contact pressures. A combination of atomic force microscopy, quartz crystal microbalance with dissipation monitoring, and friction force microscopy with soft polydimethylsiloxane (PDMS, 150 kPa) surfaces was employed to elucidate the frictional properties of model plant proteins, i.e. lupine, pea, and potato proteins at the nanoscale while systematically varying the pH and ionic strength. Interactions of these plant proteins with purified mucins were also probed. We provide the much-needed direct experimental evidence that the main factor dictating the frictional properties of plant proteins is their affinity towards the surface, followed by the degree of protein film hydration. Proteins with high surface affinity, such as pea and potato protein, have better lubricating performance than lupine at the nanoscale. Other minor factors that drive lubrication are surface interactions between sliding bodies, especially at low load, whilst jamming of the contact area caused by larger protein aggregates increases friction. Novel findings reveal that interactions between plant proteins and mucins lead to superior lubricating properties, by combining high surface affinity from the plant proteins and high hydration by mucins. We anticipate that fundamental understanding gained from this work will set the stage for the design of a plethora of sustainable biomaterials and food with optimum nanolubrication performance. RSC 2022-12-26 /pmc/articles/PMC9926882/ /pubmed/36798497 http://dx.doi.org/10.1039/d2na00696k Text en This journal is © The Royal Society of Chemistry https://creativecommons.org/licenses/by/3.0/ |
spellingShingle | Chemistry Liamas, Evangelos Connell, Simon D. Sarkar, Anwesha Frictional behaviour of plant proteins in soft contacts: unveiling nanoscale mechanisms |
title | Frictional behaviour of plant proteins in soft contacts: unveiling nanoscale mechanisms |
title_full | Frictional behaviour of plant proteins in soft contacts: unveiling nanoscale mechanisms |
title_fullStr | Frictional behaviour of plant proteins in soft contacts: unveiling nanoscale mechanisms |
title_full_unstemmed | Frictional behaviour of plant proteins in soft contacts: unveiling nanoscale mechanisms |
title_short | Frictional behaviour of plant proteins in soft contacts: unveiling nanoscale mechanisms |
title_sort | frictional behaviour of plant proteins in soft contacts: unveiling nanoscale mechanisms |
topic | Chemistry |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9926882/ https://www.ncbi.nlm.nih.gov/pubmed/36798497 http://dx.doi.org/10.1039/d2na00696k |
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