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Ted"},"authorAffiliation":{"typeName":"authorAffiliation","multiple":false,"typeClass":"primitive","value":"Biomechanics Research Centre (BioMEC), Biomedical Engineering, School of Engineering, College of Science and Engineering, University of Galway"}},{"authorName":{"typeName":"authorName","multiple":false,"typeClass":"primitive","value":"Bortesi, Luisa"},"authorAffiliation":{"typeName":"authorAffiliation","multiple":false,"typeClass":"primitive","value":"https://ror.org/02jz4aj89","expandedvalue":{"scheme":"http://www.grid.ac/ontology/","termName":"Maastricht 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The major constituent of silk is fibroin, a protein widely used in the biomedical field because of its mechanical strength, toughness and elasticity, as well as its biocompatibility and biodegradability. The domestication of silkworms allows large amounts of fibroin to be extracted inexpensively from silk cocoons. However, the industrial extraction process has drawbacks in terms of sustainability and the quality of the final medical product. The heterologous production of fibroin using recombinant DNA technology is a promising approach to address these issues, but the production of such recombinant proteins is challenging and further optimization is required due to the large size and repetitive structure of fibroin's DNA and amino acid sequence. In this review, we describe the structure–function relationship of fibroin, the current extraction process, and some insights into the sustainability of silk production for biomedical applications. We focus on recent advances in molecular biotechnology underpinning the production of recombinant fibroin, working toward a standardized, successful and sustainable process."}}]},{"typeName":"subject","multiple":true,"typeClass":"controlledVocabulary","value":["Earth and Environmental Sciences","Medicine, Health and Life Sciences"]},{"typeName":"keyword","multiple":true,"typeClass":"compound","value":[{"keywordValue":{"typeName":"keywordValue","multiple":false,"typeClass":"primitive","value":"Silk"}},{"keywordValue":{"typeName":"keywordValue","multiple":false,"typeClass":"primitive","value":"Fibroin"}},{"keywordValue":{"typeName":"keywordValue","multiple":false,"typeClass":"primitive","value":"Structure"}},{"keywordValue":{"typeName":"keywordValue","multiple":false,"typeClass":"primitive","value":"Sustainability"}},{"keywordValue":{"typeName":"keywordValue","multiple":false,"typeClass":"primitive","value":"Biomedical applications"}},{"keywordValue":{"typeName":"keywordValue","multiple":false,"typeClass":"primitive","value":"Biotechnology"}},{"keywordValue":{"typeName":"keywordValue","multiple":false,"typeClass":"primitive","value":"Recombinant protein"}},{"keywordValue":{"typeName":"keywordValue","multiple":false,"typeClass":"primitive","value":"Heterologous protein production"}}]},{"typeName":"grantNumber","multiple":true,"typeClass":"compound","value":[{"grantNumberAgency":{"typeName":"grantNumberAgency","multiple":false,"typeClass":"primitive","value":"European Union's Horizon 2020 research and innovation programme under Marie Skolodowska-Curie grant"},"grantNumberValue":{"typeName":"grantNumberValue","multiple":false,"typeClass":"primitive","value":"ID: 956621"}}]},{"typeName":"distributor","multiple":true,"typeClass":"compound","value":[{"distributorName":{"typeName":"distributorName","multiple":false,"typeClass":"primitive","value":"International Journal of Biological Macromolecules"},"distributorAffiliation":{"typeName":"distributorAffiliation","multiple":false,"typeClass":"primitive","value":"Elsevier"},"distributorURL":{"typeName":"distributorURL","multiple":false,"typeClass":"primitive","value":"https://www.sciencedirect.com/journal/international-journal-of-biological-macromolecules"}}]},{"typeName":"distributionDate","multiple":false,"typeClass":"primitive","value":"2024-02-24"},{"typeName":"depositor","multiple":false,"typeClass":"primitive","value":"Bitar, Lara"},{"typeName":"dateOfDeposit","multiple":false,"typeClass":"primitive","value":"2025-03-26"}]},"dansDataVaultMetadata":{"displayName":"Data Vault Metadata","name":"dansDataVaultMetadata","fields":[{"typeName":"dansDataversePid","multiple":false,"typeClass":"primitive","value":"doi:10.34894/MCA5MR"},{"typeName":"dansDataversePidVersion","multiple":false,"typeClass":"primitive","value":"1.0"},{"typeName":"dansBagId","multiple":false,"typeClass":"primitive","value":"urn:uuid:b04244ce-d2e2-4e7e-9d1a-f58f1b1025f9"},{"typeName":"dansNbn","multiple":false,"typeClass":"primitive","value":"urn:nbn:nl:ui:13-2a2223a8-ab1a-43e7-b830-245ed6d294a3"}]}},"files":[{"label":"1-s2.0-S0141813024011772-main-1.pdf","restricted":false,"version":1,"datasetVersionId":30406,"dataFile":{"id":478211,"persistentId":"","filename":"1-s2.0-S0141813024011772-main-1.pdf","contentType":"application/pdf","friendlyType":"Adobe PDF","filesize":2198652,"storageIdentifier":"surf://store:195d2d967e9-22efdbddb85a","rootDataFileId":-1,"checksum":{"type":"SHA-1","value":"cd96ce191b1e1f94dd8907e1472ed8d0d3b5e296"},"tabularData":false,"creationDate":"2025-03-26","publicationDate":"2025-03-27","lastUpdateTime":"2025-03-27T11:21:59Z","fileAccessRequest":true}},{"label":"Bibliography- francesca.bib","restricted":false,"version":1,"datasetVersionId":30406,"dataFile":{"id":478260,"persistentId":"","filename":"Bibliography- francesca.bib","contentType":"application/octet-stream","friendlyType":"Unknown","filesize":27838,"storageIdentifier":"surf://store:195d727fd8d-62db72b5e3b1","rootDataFileId":-1,"checksum":{"type":"SHA-1","value":"7bad8b2912dfc8e3294c6ec98104d909bee13f09"},"tabularData":false,"creationDate":"2025-03-27","publicationDate":"2025-03-27","lastUpdateTime":"2025-03-27T11:21:59Z","fileAccessRequest":true}},{"description":"Fig. 1. The three-level hierarchical structure of silk fibers. Reproduced with permission (copyright 2020, Wiley-VCH [13]).","label":"Fig 1.jpg","restricted":false,"version":1,"datasetVersionId":30406,"dataFile":{"id":478252,"persistentId":"","filename":"Fig 1.jpg","contentType":"image/jpeg","friendlyType":"JPEG Image","filesize":2914567,"description":"Fig. 1. The three-level hierarchical structure of silk fibers. Reproduced with permission (copyright 2020, Wiley-VCH [13]).","storageIdentifier":"surf://store:195d71f4379-f616d5b7749e","rootDataFileId":-1,"checksum":{"type":"SHA-1","value":"f74ab78b1dc60c3fa6db3ff3b2711a098629e632"},"tabularData":false,"creationDate":"2025-03-27","publicationDate":"2025-03-27","lastUpdateTime":"2025-03-27T11:21:59Z","fileAccessRequest":true}},{"description":"Fig. 2. The repetitive nature of the fibroin heavy chain (H-Fb) amino acid sequence. The 12 repetitive domains are separated by 11 amorphous motifs and flanked by\nN-terminal and C-terminal sequences that facilitate assembly into a heteropolymer with the fibroin light chain (L-Fb). Multiple motifs of repetitive amino acid\nsequences make up each repetitive domain.","label":"Fig 2.jpg","restricted":false,"version":1,"datasetVersionId":30406,"dataFile":{"id":478253,"persistentId":"","filename":"Fig 2.jpg","contentType":"image/jpeg","friendlyType":"JPEG Image","filesize":1998608,"description":"Fig. 2. The repetitive nature of the fibroin heavy chain (H-Fb) amino acid sequence. The 12 repetitive domains are separated by 11 amorphous motifs and flanked by\nN-terminal and C-terminal sequences that facilitate assembly into a heteropolymer with the fibroin light chain (L-Fb). Multiple motifs of repetitive amino acid\nsequences make up each repetitive domain.","storageIdentifier":"surf://store:195d71f5079-7ab025e195f5","rootDataFileId":-1,"checksum":{"type":"SHA-1","value":"8ce5990f868b33e52f8b89af33f6a2ff53980b9b"},"tabularData":false,"creationDate":"2025-03-27","publicationDate":"2025-03-27","lastUpdateTime":"2025-03-27T11:21:59Z","fileAccessRequest":true}},{"description":"Fig. 3. Natural production of silk. Stage 1: in the posterior silk gland (PSG), the fibroin complex is assembled from its three components (the light and heavy fibroin\nchains and the glycoprotein P25). Stage 2: in the middle silk gland (MSG), a sericin coating is deposited on the fibroin complex to form the silk protein. Stage 3: in the\nanterior silk gland (ASG), silk fibers are assembled from individual silk protein complexes. Stage 4: silk fibers are matured in Filippi's glands. Stage 5: silk fibers are\nspun and secreted from the spinneret. (Adapted from [25]).","label":"Fig 3.jpg","restricted":false,"version":1,"datasetVersionId":30406,"dataFile":{"id":478250,"persistentId":"","filename":"Fig 3.jpg","contentType":"image/jpeg","friendlyType":"JPEG Image","filesize":1369609,"description":"Fig. 3. Natural production of silk. Stage 1: in the posterior silk gland (PSG), the fibroin complex is assembled from its three components (the light and heavy fibroin\nchains and the glycoprotein P25). Stage 2: in the middle silk gland (MSG), a sericin coating is deposited on the fibroin complex to form the silk protein. Stage 3: in the\nanterior silk gland (ASG), silk fibers are assembled from individual silk protein complexes. Stage 4: silk fibers are matured in Filippi's glands. Stage 5: silk fibers are\nspun and secreted from the spinneret. (Adapted from [25]).","storageIdentifier":"surf://store:195d71f5d2e-ec4c70f11649","rootDataFileId":-1,"checksum":{"type":"SHA-1","value":"2858261362ccb5db59a32b711289d2f98f0b205e"},"tabularData":false,"creationDate":"2025-03-27","publicationDate":"2025-03-27","lastUpdateTime":"2025-03-27T11:21:59Z","fileAccessRequest":true}},{"description":"Fig. 4. Stress–strain behavior of most spider silks. (a) Generic stress–strain diagram describing the behavior of defect-free silk under an external force (redrawn from\n[39]). (b) Four different regimes of mechanical behavior: (I) linear elastic, (II) unfolding plateau, (III) stiffening, and (IV) softening.","label":"Fig 4 a.jpg","restricted":false,"version":1,"datasetVersionId":30406,"dataFile":{"id":478254,"persistentId":"","filename":"Fig 4 a.jpg","contentType":"image/jpeg","friendlyType":"JPEG Image","filesize":681408,"description":"Fig. 4. Stress–strain behavior of most spider silks. (a) Generic stress–strain diagram describing the behavior of defect-free silk under an external force (redrawn from\n[39]). (b) Four different regimes of mechanical behavior: (I) linear elastic, (II) unfolding plateau, (III) stiffening, and (IV) softening.","storageIdentifier":"surf://store:195d71f64e6-c40e68bb9e9b","rootDataFileId":-1,"checksum":{"type":"SHA-1","value":"0d37a3754efe40082936910a6f0492931d1bcb0f"},"tabularData":false,"creationDate":"2025-03-27","publicationDate":"2025-03-27","lastUpdateTime":"2025-03-27T11:21:59Z","fileAccessRequest":true}},{"description":"Fig. 4. Stress–strain behavior of most spider silks. (a) Generic stress–strain diagram describing the behavior of defect-free silk under an external force (redrawn from\n[39]). (b) Four different regimes of mechanical behavior: (I) linear elastic, (II) unfolding plateau, (III) stiffening, and (IV) softening.","label":"Fig 4 b.jpg","restricted":false,"version":1,"datasetVersionId":30406,"dataFile":{"id":478257,"persistentId":"","filename":"Fig 4 b.jpg","contentType":"image/jpeg","friendlyType":"JPEG Image","filesize":740138,"description":"Fig. 4. Stress–strain behavior of most spider silks. (a) Generic stress–strain diagram describing the behavior of defect-free silk under an external force (redrawn from\n[39]). (b) Four different regimes of mechanical behavior: (I) linear elastic, (II) unfolding plateau, (III) stiffening, and (IV) softening.","storageIdentifier":"surf://store:195d71f6d0d-18890c034a34","rootDataFileId":-1,"checksum":{"type":"SHA-1","value":"38dc538102e9e7ceb29f0d6f09996c6a62938776"},"tabularData":false,"creationDate":"2025-03-27","publicationDate":"2025-03-27","lastUpdateTime":"2025-03-27T11:21:59Z","fileAccessRequest":true}},{"description":"Fig. 5. Comparative stress–strain curves for single filaments of silk from the\nsilkworm Bombyx mori and the spider Nephila edulis (adapted with permission\n[43], copyright 2003 American Chemical Society). [49].","label":"Fig 5.jpg","restricted":false,"version":1,"datasetVersionId":30406,"dataFile":{"id":478251,"persistentId":"","filename":"Fig 5.jpg","contentType":"image/jpeg","friendlyType":"JPEG Image","filesize":641117,"description":"Fig. 5. Comparative stress–strain curves for single filaments of silk from the\nsilkworm Bombyx mori and the spider Nephila edulis (adapted with permission\n[43], copyright 2003 American Chemical Society). [49].","storageIdentifier":"surf://store:195d71f753e-04c27297965c","rootDataFileId":-1,"checksum":{"type":"SHA-1","value":"c258cc9fbf71a96f5010c6e08528542a9dc12cde"},"tabularData":false,"creationDate":"2025-03-27","publicationDate":"2025-03-27","lastUpdateTime":"2025-03-27T11:21:59Z","fileAccessRequest":true}},{"description":"Fig. 6. The main steps required to extract silk fibroin from silkworm cocoons and the corresponding performance-related and sustainability issues and\npossible solutions.","label":"Fig 6.jpg","restricted":false,"version":1,"datasetVersionId":30406,"dataFile":{"id":478256,"persistentId":"","filename":"Fig 6.jpg","contentType":"image/jpeg","friendlyType":"JPEG Image","filesize":1377522,"description":"Fig. 6. The main steps required to extract silk fibroin from silkworm cocoons and the corresponding performance-related and sustainability issues and\npossible solutions.","storageIdentifier":"surf://store:195d71f7bdb-8e233f7783d1","rootDataFileId":-1,"checksum":{"type":"SHA-1","value":"d116fd338f396a6e52eddad1e514823dd7a0945a"},"tabularData":false,"creationDate":"2025-03-27","publicationDate":"2025-03-27","lastUpdateTime":"2025-03-27T11:21:59Z","fileAccessRequest":true}},{"description":"Silk is a natural engineering material with a unique set of properties. The major constituent of silk is fibroin, a\nprotein widely used in the biomedical field because of its mechanical strength, toughness and elasticity, as well\nas its biocompatibility and biodegradability. The domestication of silkworms allows large amounts of fibroin to\nbe extracted inexpensively from silk cocoons. However, the industrial extraction process has drawbacks in terms\nof sustainability and the quality of the final medical product. The heterologous production of fibroin using recombinant\nDNA technology is a promising approach to address these issues, but the production of such recombinant\nproteins is challenging and further optimization is required due to the large size and repetitive\nstructure of fibroin's DNA and amino acid sequence. In this review, we describe the structure–function relationship\nof fibroin, the current extraction process, and some insights into the sustainability of silk production for\nbiomedical applications. We focus on recent advances in molecular biotechnology underpinning the production\nof recombinant fibroin, working toward a standardized, successful and sustainable process.","label":"Graphical abstract.jpg","restricted":false,"version":1,"datasetVersionId":30406,"dataFile":{"id":478255,"persistentId":"","filename":"Graphical abstract.jpg","contentType":"image/jpeg","friendlyType":"JPEG Image","filesize":4394793,"description":"Silk is a natural engineering material with a unique set of properties. The major constituent of silk is fibroin, a\nprotein widely used in the biomedical field because of its mechanical strength, toughness and elasticity, as well\nas its biocompatibility and biodegradability. The domestication of silkworms allows large amounts of fibroin to\nbe extracted inexpensively from silk cocoons. However, the industrial extraction process has drawbacks in terms\nof sustainability and the quality of the final medical product. The heterologous production of fibroin using recombinant\nDNA technology is a promising approach to address these issues, but the production of such recombinant\nproteins is challenging and further optimization is required due to the large size and repetitive\nstructure of fibroin's DNA and amino acid sequence. In this review, we describe the structure–function relationship\nof fibroin, the current extraction process, and some insights into the sustainability of silk production for\nbiomedical applications. We focus on recent advances in molecular biotechnology underpinning the production\nof recombinant fibroin, working toward a standardized, successful and sustainable process.","storageIdentifier":"surf://store:195d71f802c-4d860b3a1c47","rootDataFileId":-1,"checksum":{"type":"SHA-1","value":"dbdeba8375aaa8db99b39b16ff5cef869c6af31b"},"tabularData":false,"creationDate":"2025-03-27","publicationDate":"2025-03-27","lastUpdateTime":"2025-03-27T11:21:59Z","fileAccessRequest":true}},{"label":"library lara new.bib","restricted":false,"version":1,"datasetVersionId":30406,"dataFile":{"id":478259,"persistentId":"","filename":"library lara new.bib","contentType":"application/octet-stream","friendlyType":"Unknown","filesize":507526,"storageIdentifier":"surf://store:195d727fe37-c52a5fbf06ad","rootDataFileId":-1,"checksum":{"type":"SHA-1","value":"8898a6b240a4817789198b4b01420a42dbc697f0"},"tabularData":false,"creationDate":"2025-03-27","publicationDate":"2025-03-27","lastUpdateTime":"2025-03-27T11:21:59Z","fileAccessRequest":true}},{"label":"Old draft-Sustainable Bombyx moris silk fibroin for biomedical applications a molecular biotechnology challenge.DOCX","restricted":false,"version":1,"datasetVersionId":30406,"dataFile":{"id":478258,"persistentId":"","filename":"Old draft-Sustainable Bombyx moris silk fibroin for biomedical applications a molecular biotechnology challenge.DOCX","contentType":"application/vnd.openxmlformats-officedocument.wordprocessingml.document","friendlyType":"MS Word","filesize":2732765,"storageIdentifier":"surf://store:195d726f44b-2132b0c2427d","rootDataFileId":-1,"checksum":{"type":"SHA-1","value":"154236308c16780cbe4b27def1124eff41942e10"},"tabularData":false,"creationDate":"2025-03-27","publicationDate":"2025-03-27","lastUpdateTime":"2025-03-27T11:21:59Z","fileAccessRequest":true}},{"label":"Tables word format.DOCX","restricted":false,"version":1,"datasetVersionId":30406,"dataFile":{"id":478261,"persistentId":"","filename":"Tables word format.DOCX","contentType":"application/vnd.openxmlformats-officedocument.wordprocessingml.document","friendlyType":"MS Word","filesize":926413,"storageIdentifier":"surf://store:195d7260eaf-3dcfecb1575d","rootDataFileId":-1,"checksum":{"type":"SHA-1","value":"b7733bb8b6524c69f2c709347a16d900aca168fa"},"tabularData":false,"creationDate":"2025-03-27","publicationDate":"2025-03-27","lastUpdateTime":"2025-03-27T11:21:59Z","fileAccessRequest":true}}]}}}