Exploration of the hierarchical assembly space of collagen-like peptides beyond the triple helix
Abstract The de novo design of self-assembling peptides has garnered significant attention in scientific research. While alpha-helical assemblies have been extensively studied, exploration of polyproline type II helices, such as those found in collagen, remains relatively limited. In this study, we...
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| Format: | Article |
| Language: | English |
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Nature Portfolio
2024-11-01
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| Series: | Nature Communications |
| Online Access: | https://doi.org/10.1038/s41467-024-54560-z |
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| author | Le Tracy Yu Mark A. B. Kreutzberger Thi H. Bui Maria C. Hancu Adam C. Farsheed Edward H. Egelman Jeffrey D. Hartgerink |
| author_facet | Le Tracy Yu Mark A. B. Kreutzberger Thi H. Bui Maria C. Hancu Adam C. Farsheed Edward H. Egelman Jeffrey D. Hartgerink |
| author_sort | Le Tracy Yu |
| collection | DOAJ |
| description | Abstract The de novo design of self-assembling peptides has garnered significant attention in scientific research. While alpha-helical assemblies have been extensively studied, exploration of polyproline type II helices, such as those found in collagen, remains relatively limited. In this study, we focus on understanding the sequence-structure relationship in hierarchical assemblies of collagen-like peptides, using defense collagen Surfactant Protein A as a model. By dissecting the sequence derived from Surfactant Protein A and synthesizing short collagen-like peptides, we successfully construct a discrete bundle of hollow triple helices. Amino acid substitution studies pinpoint hydrophobic and charged residues that are critical for oligomer formation. These insights guide the de novo design of collagen-like peptides, resulting in the formation of diverse quaternary structures, including discrete and heterogenous bundled oligomers, two-dimensional nanosheets, and pH-responsive nanoribbons. Our study represents a significant advancement in the understanding and harnessing of collagen higher-order assemblies beyond the triple helix. |
| format | Article |
| id | doaj-art-7ce13761d93c4daeb9d9e44a625ead58 |
| institution | Kabale University |
| issn | 2041-1723 |
| language | English |
| publishDate | 2024-11-01 |
| publisher | Nature Portfolio |
| record_format | Article |
| series | Nature Communications |
| spelling | doaj-art-7ce13761d93c4daeb9d9e44a625ead582024-12-01T12:35:39ZengNature PortfolioNature Communications2041-17232024-11-0115111110.1038/s41467-024-54560-zExploration of the hierarchical assembly space of collagen-like peptides beyond the triple helixLe Tracy Yu0Mark A. B. Kreutzberger1Thi H. Bui2Maria C. Hancu3Adam C. Farsheed4Edward H. Egelman5Jeffrey D. Hartgerink6Department of Chemistry, Rice UniversityDepartment of Biochemistry and Molecular Genetics, University of Virginia School of MedicineDepartment of Chemistry, Rice UniversityDepartment of Chemistry, Rice UniversityDepartment of Bioengineering, Rice UniversityDepartment of Biochemistry and Molecular Genetics, University of Virginia School of MedicineDepartment of Chemistry, Rice UniversityAbstract The de novo design of self-assembling peptides has garnered significant attention in scientific research. While alpha-helical assemblies have been extensively studied, exploration of polyproline type II helices, such as those found in collagen, remains relatively limited. In this study, we focus on understanding the sequence-structure relationship in hierarchical assemblies of collagen-like peptides, using defense collagen Surfactant Protein A as a model. By dissecting the sequence derived from Surfactant Protein A and synthesizing short collagen-like peptides, we successfully construct a discrete bundle of hollow triple helices. Amino acid substitution studies pinpoint hydrophobic and charged residues that are critical for oligomer formation. These insights guide the de novo design of collagen-like peptides, resulting in the formation of diverse quaternary structures, including discrete and heterogenous bundled oligomers, two-dimensional nanosheets, and pH-responsive nanoribbons. Our study represents a significant advancement in the understanding and harnessing of collagen higher-order assemblies beyond the triple helix.https://doi.org/10.1038/s41467-024-54560-z |
| spellingShingle | Le Tracy Yu Mark A. B. Kreutzberger Thi H. Bui Maria C. Hancu Adam C. Farsheed Edward H. Egelman Jeffrey D. Hartgerink Exploration of the hierarchical assembly space of collagen-like peptides beyond the triple helix Nature Communications |
| title | Exploration of the hierarchical assembly space of collagen-like peptides beyond the triple helix |
| title_full | Exploration of the hierarchical assembly space of collagen-like peptides beyond the triple helix |
| title_fullStr | Exploration of the hierarchical assembly space of collagen-like peptides beyond the triple helix |
| title_full_unstemmed | Exploration of the hierarchical assembly space of collagen-like peptides beyond the triple helix |
| title_short | Exploration of the hierarchical assembly space of collagen-like peptides beyond the triple helix |
| title_sort | exploration of the hierarchical assembly space of collagen like peptides beyond the triple helix |
| url | https://doi.org/10.1038/s41467-024-54560-z |
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