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An essential role of disulfide bonds for the hierarchical self-assembly and underwater affinity of CP20-derived peptides
Barnacles are typical fouling organisms strongly adhere to immersed solid substrates by secreting proteinaceous adhesives called cement proteins (CPs). The self-assembly of the CPs forms a permanently bonded layer that binds barnacles to foreign surfaces. However, it is difficult to determine their...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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Frontiers Media S.A.
2022
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9597634/ https://www.ncbi.nlm.nih.gov/pubmed/36312552 http://dx.doi.org/10.3389/fbioe.2022.998194 |
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author | Li, Baoshan Song, Junyi Mao, Ting Zeng, Ling Ye, Zonghuang Hu, Biru |
author_facet | Li, Baoshan Song, Junyi Mao, Ting Zeng, Ling Ye, Zonghuang Hu, Biru |
author_sort | Li, Baoshan |
collection | PubMed |
description | Barnacles are typical fouling organisms strongly adhere to immersed solid substrates by secreting proteinaceous adhesives called cement proteins (CPs). The self-assembly of the CPs forms a permanently bonded layer that binds barnacles to foreign surfaces. However, it is difficult to determine their natural structure and describe their self-assembly properties due to the abundance of cysteines in whole-length CP20. A putative functional motif of Balanus albicostatus CP20 (BalCP20) was identified to present distinctive self-assembly and wet-binding characteristics. Atomic-force microscopy (AFM) and transmission electron microscope (TEM) investigations showed that wildtype BalCP20-P3 formed grain-like spindles, which assembled into fractal-like structures like ears of wheat. SDS-PAGE, AFM, and LSCM showed that DTT treatment opened up disulfide bonds between cysteines and disrupted fractal-like structures. Additionally, these morphologies were abolished when one of the BalCP20-P3 four cysteines was mutated by alanine. Circular dichroism (CD) results suggested that the morphological diversity among BalCP20-P3 and its mutations was related to the proportion of α-helices. Finally, quartz crystal microbalance with dissipation (QCM-D) detected that BalCP20-P3 and its mutations with diverse self-assemblies occupied different affinities. The above results demonstrated that cysteines and disulfide bonds played a crucial role in the self-assembly and wet binding of BalCP20-P3. The work provides new ideas for the underwater bonding of BalCP20 and developing new bionic underwater adhesives. |
format | Online Article Text |
id | pubmed-9597634 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | Frontiers Media S.A. |
record_format | MEDLINE/PubMed |
spelling | pubmed-95976342022-10-27 An essential role of disulfide bonds for the hierarchical self-assembly and underwater affinity of CP20-derived peptides Li, Baoshan Song, Junyi Mao, Ting Zeng, Ling Ye, Zonghuang Hu, Biru Front Bioeng Biotechnol Bioengineering and Biotechnology Barnacles are typical fouling organisms strongly adhere to immersed solid substrates by secreting proteinaceous adhesives called cement proteins (CPs). The self-assembly of the CPs forms a permanently bonded layer that binds barnacles to foreign surfaces. However, it is difficult to determine their natural structure and describe their self-assembly properties due to the abundance of cysteines in whole-length CP20. A putative functional motif of Balanus albicostatus CP20 (BalCP20) was identified to present distinctive self-assembly and wet-binding characteristics. Atomic-force microscopy (AFM) and transmission electron microscope (TEM) investigations showed that wildtype BalCP20-P3 formed grain-like spindles, which assembled into fractal-like structures like ears of wheat. SDS-PAGE, AFM, and LSCM showed that DTT treatment opened up disulfide bonds between cysteines and disrupted fractal-like structures. Additionally, these morphologies were abolished when one of the BalCP20-P3 four cysteines was mutated by alanine. Circular dichroism (CD) results suggested that the morphological diversity among BalCP20-P3 and its mutations was related to the proportion of α-helices. Finally, quartz crystal microbalance with dissipation (QCM-D) detected that BalCP20-P3 and its mutations with diverse self-assemblies occupied different affinities. The above results demonstrated that cysteines and disulfide bonds played a crucial role in the self-assembly and wet binding of BalCP20-P3. The work provides new ideas for the underwater bonding of BalCP20 and developing new bionic underwater adhesives. Frontiers Media S.A. 2022-10-12 /pmc/articles/PMC9597634/ /pubmed/36312552 http://dx.doi.org/10.3389/fbioe.2022.998194 Text en Copyright © 2022 Li, Song, Mao, Zeng, Ye and Hu. https://creativecommons.org/licenses/by/4.0/This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms. |
spellingShingle | Bioengineering and Biotechnology Li, Baoshan Song, Junyi Mao, Ting Zeng, Ling Ye, Zonghuang Hu, Biru An essential role of disulfide bonds for the hierarchical self-assembly and underwater affinity of CP20-derived peptides |
title | An essential role of disulfide bonds for the hierarchical self-assembly and underwater affinity of CP20-derived peptides |
title_full | An essential role of disulfide bonds for the hierarchical self-assembly and underwater affinity of CP20-derived peptides |
title_fullStr | An essential role of disulfide bonds for the hierarchical self-assembly and underwater affinity of CP20-derived peptides |
title_full_unstemmed | An essential role of disulfide bonds for the hierarchical self-assembly and underwater affinity of CP20-derived peptides |
title_short | An essential role of disulfide bonds for the hierarchical self-assembly and underwater affinity of CP20-derived peptides |
title_sort | essential role of disulfide bonds for the hierarchical self-assembly and underwater affinity of cp20-derived peptides |
topic | Bioengineering and Biotechnology |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9597634/ https://www.ncbi.nlm.nih.gov/pubmed/36312552 http://dx.doi.org/10.3389/fbioe.2022.998194 |
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