{"record_type":"pith_number_record","schema_url":"https://pith.science/schemas/pith-number/v1.json","pith_number":"pith:2025:SSBBJLCABVNKZBYJKEOAGALKKW","short_pith_number":"pith:SSBBJLCA","schema_version":"1.0","canonical_sha256":"948214ac400d5aac8709511c03016a558354e719dc03635d26f2f5f5721e27ca","source":{"kind":"arxiv","id":"2507.14577","version":1},"attestation_state":"computed","paper":{"title":"De novo design of alpha-helical peptide amphiphiles repairing fragmented collagen type I via supramolecular co-assembly","license":"http://arxiv.org/licenses/nonexclusive-distrib/1.0/","headline":"","cross_cats":[],"primary_cat":"physics.chem-ph","authors_text":"Alexander van Teijlingen, Dawen Yu, Guo Zhang, Haoran Zhang, Hua Yang, Jialong Chen, Jiaming Sun, Jie Yang, Shanshan Su, Tong Li, Yuanhao Wu, Yubin Ke, Yuxuan Chen, Zhiquan Yu","submitted_at":"2025-07-19T11:30:00Z","abstract_excerpt":"The hierarchical triple-helix structure of collagen type I, Col I, is essential for extracellular matrix support and integrity. However, current reconstruction strategies face challenges such as chain mismatch, preventing proper fibril formation. Here, we report a supramolecular co-assembly strategy using a de novo-designed alpha-helical peptide amphiphile (APA) of just seven amino acids. The APA features a hydrophobic palmitic acid tail, which stabilizes the helical structure and promotes co-assembly upon interaction with complementary molecular structures. This minimal design enables selecti"},"verification_status":{"content_addressed":true,"pith_receipt":true,"author_attested":false,"weak_author_claims":0,"strong_author_claims":0,"externally_anchored":false,"storage_verified":false,"citation_signatures":0,"replication_records":0,"graph_snapshot":true,"references_resolved":false,"formal_links_present":false},"canonical_record":{"source":{"id":"2507.14577","kind":"arxiv","version":1},"metadata":{"license":"http://arxiv.org/licenses/nonexclusive-distrib/1.0/","primary_cat":"physics.chem-ph","submitted_at":"2025-07-19T11:30:00Z","cross_cats_sorted":[],"title_canon_sha256":"aaf9fb2c80c5afe46d6ab61942deef33bb3f117b0ded46b4b2100c782ca0dbee","abstract_canon_sha256":"97fa4a601aa15f95b6d9e3067e3b41ea1c76a3e6d7b525eee8401871915cb1ae"},"schema_version":"1.0"},"receipt":{"kind":"pith_receipt","key_id":"pith-v1-2026-05","algorithm":"ed25519","signed_at":"2026-07-05T11:40:09.773796Z","signature_b64":"EDM0YNgku5rffCiTy1xhKyBd4es3pfVa0ofUSYHTGqjSmlE3wfR94u9Uz2DrYRUnxyuMcVd1MA9M6i110kdABw==","signed_message":"canonical_sha256_bytes","builder_version":"pith-number-builder-2026-05-17-v1","receipt_version":"0.3","canonical_sha256":"948214ac400d5aac8709511c03016a558354e719dc03635d26f2f5f5721e27ca","last_reissued_at":"2026-07-05T11:40:09.773268Z","signature_status":"signed_v1","first_computed_at":"2026-07-05T11:40:09.773268Z","public_key_fingerprint":"8d4b5ee74e4693bcd1df2446408b0d54"},"graph_snapshot":{"paper":{"title":"De novo design of alpha-helical peptide amphiphiles repairing fragmented collagen type I via supramolecular co-assembly","license":"http://arxiv.org/licenses/nonexclusive-distrib/1.0/","headline":"","cross_cats":[],"primary_cat":"physics.chem-ph","authors_text":"Alexander van Teijlingen, Dawen Yu, Guo Zhang, Haoran Zhang, Hua Yang, Jialong Chen, Jiaming Sun, Jie Yang, Shanshan Su, Tong Li, Yuanhao Wu, Yubin Ke, Yuxuan Chen, Zhiquan Yu","submitted_at":"2025-07-19T11:30:00Z","abstract_excerpt":"The hierarchical triple-helix structure of collagen type I, Col I, is essential for extracellular matrix support and integrity. However, current reconstruction strategies face challenges such as chain mismatch, preventing proper fibril formation. Here, we report a supramolecular co-assembly strategy using a de novo-designed alpha-helical peptide amphiphile (APA) of just seven amino acids. The APA features a hydrophobic palmitic acid tail, which stabilizes the helical structure and promotes co-assembly upon interaction with complementary molecular structures. This minimal design enables selecti"},"claims":{"count":0,"items":[],"snapshot_sha256":"258153158e38e3291e3d48162225fcdb2d5a3ed65a07baac614ab91432fd4f57"},"source":{"id":"2507.14577","kind":"arxiv","version":1},"verdict":{"id":null,"model_set":{},"created_at":null,"strongest_claim":"","one_line_summary":"","pipeline_version":null,"weakest_assumption":"","pith_extraction_headline":""},"integrity":{"clean":true,"summary":{"advisory":0,"critical":0,"by_detector":{},"informational":0},"endpoint":"/pith/2507.14577/integrity.json","findings":[],"available":true,"detectors_run":[],"snapshot_sha256":"c28c3603d3b5d939e8dc4c7e95fa8dfce3d595e45f758748cecf8e644a296938"},"references":{"count":0,"sample":[],"resolved_work":0,"snapshot_sha256":"258153158e38e3291e3d48162225fcdb2d5a3ed65a07baac614ab91432fd4f57","internal_anchors":0},"formal_canon":{"evidence_count":0,"snapshot_sha256":"258153158e38e3291e3d48162225fcdb2d5a3ed65a07baac614ab91432fd4f57"},"author_claims":{"count":0,"strong_count":0,"snapshot_sha256":"258153158e38e3291e3d48162225fcdb2d5a3ed65a07baac614ab91432fd4f57"},"builder_version":"pith-number-builder-2026-05-17-v1"},"aliases":[{"alias_kind":"arxiv","alias_value":"2507.14577","created_at":"2026-07-05T11:40:09.773338+00:00"},{"alias_kind":"arxiv_version","alias_value":"2507.14577v1","created_at":"2026-07-05T11:40:09.773338+00:00"},{"alias_kind":"doi","alias_value":"10.48550/arxiv.2507.14577","created_at":"2026-07-05T11:40:09.773338+00:00"},{"alias_kind":"pith_short_12","alias_value":"SSBBJLCABVNK","created_at":"2026-07-05T11:40:09.773338+00:00"},{"alias_kind":"pith_short_16","alias_value":"SSBBJLCABVNKZBYJ","created_at":"2026-07-05T11:40:09.773338+00:00"},{"alias_kind":"pith_short_8","alias_value":"SSBBJLCA","created_at":"2026-07-05T11:40:09.773338+00:00"}],"events":[],"event_summary":{},"paper_claims":[],"inbound_citations":{"count":1,"internal_anchor_count":0,"sample":[{"citing_arxiv_id":"2604.23945","citing_title":"An in situ self-adaptive hydrogel coating enables seamless neural interfaces via okra mucilage polysaccharide and {\\alpha}-helical peptide amphiphiles co-assembly","ref_index":48,"is_internal_anchor":false}]},"formal_canon":{"evidence_count":0,"sample":[],"anchors":[]},"links":{"html":"https://pith.science/pith/SSBBJLCABVNKZBYJKEOAGALKKW","json":"https://pith.science/pith/SSBBJLCABVNKZBYJKEOAGALKKW.json","graph_json":"https://pith.science/api/pith-number/SSBBJLCABVNKZBYJKEOAGALKKW/graph.json","events_json":"https://pith.science/api/pith-number/SSBBJLCABVNKZBYJKEOAGALKKW/events.json","paper":"https://pith.science/paper/SSBBJLCA"},"agent_actions":{"view_html":"https://pith.science/pith/SSBBJLCABVNKZBYJKEOAGALKKW","download_json":"https://pith.science/pith/SSBBJLCABVNKZBYJKEOAGALKKW.json","view_paper":"https://pith.science/paper/SSBBJLCA","resolve_alias":"https://pith.science/api/pith-number/resolve?arxiv=2507.14577&json=true","fetch_graph":"https://pith.science/api/pith-number/SSBBJLCABVNKZBYJKEOAGALKKW/graph.json","fetch_events":"https://pith.science/api/pith-number/SSBBJLCABVNKZBYJKEOAGALKKW/events.json","actions":{"anchor_timestamp":"https://pith.science/pith/SSBBJLCABVNKZBYJKEOAGALKKW/action/timestamp_anchor","attest_storage":"https://pith.science/pith/SSBBJLCABVNKZBYJKEOAGALKKW/action/storage_attestation","attest_author":"https://pith.science/pith/SSBBJLCABVNKZBYJKEOAGALKKW/action/author_attestation","sign_citation":"https://pith.science/pith/SSBBJLCABVNKZBYJKEOAGALKKW/action/citation_signature","submit_replication":"https://pith.science/pith/SSBBJLCABVNKZBYJKEOAGALKKW/action/replication_record"}},"created_at":"2026-07-05T11:40:09.773338+00:00","updated_at":"2026-07-05T11:40:09.773338+00:00"}