{"record_type":"pith_number_record","schema_url":"https://pith.science/schemas/pith-number/v1.json","pith_number":"pith:2020:JOVVO54UJ4DWACJS35FEI2BP2M","short_pith_number":"pith:JOVVO54U","schema_version":"1.0","canonical_sha256":"4bab5777944f07600932df4a44682fd3396f12b3bfb22b4196c884fbfbbe2b6e","source":{"kind":"arxiv","id":"2005.13389","version":1},"attestation_state":"computed","paper":{"title":"Inhibiting amyloid-like aggregation through bio-conjugation of proteins with polymer surfactant","license":"http://creativecommons.org/licenses/by/4.0/","headline":"","cross_cats":["cond-mat.soft","physics.bio-ph"],"primary_cat":"q-bio.BM","authors_text":"Anasua Mukhopadhyay, David A. King, Erika Eiser, Iliya D. Stoev, Kamendra P. Sharma","submitted_at":"2020-05-27T14:42:09Z","abstract_excerpt":"Prevention of protein aggregation and thus stabilization of proteins has large biological and biotechnological implications. Here, we show that inhibition of amyloid-like aggregates is possible in stoichiometric conjugates of polymer surfactant and bovine serum albumin (BSA) chosen as a model protein. We investigate using a combination of Thioflavin-T fluorescence spectroscopy, dynamic light scattering and FTIR spectroscopy the aggregation behavior in polymer surfactant modified and unmodified (native) BSA solutions. The BSA-polymer surfactant conjugates are stable up to 5 days under aggregati"},"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":"2005.13389","kind":"arxiv","version":1},"metadata":{"license":"http://creativecommons.org/licenses/by/4.0/","primary_cat":"q-bio.BM","submitted_at":"2020-05-27T14:42:09Z","cross_cats_sorted":["cond-mat.soft","physics.bio-ph"],"title_canon_sha256":"f85d4547bd919a46d7fe5bf028021de80b41675ec3a96905606b859ac1c4e603","abstract_canon_sha256":"8030f8ec705dc331aeb5cb76de2af117b53c40a6c517e6c104c5a61c193c52f2"},"schema_version":"1.0"},"receipt":{"kind":"pith_receipt","key_id":"pith-v1-2026-05","algorithm":"ed25519","signed_at":"2026-07-05T01:06:15.529674Z","signature_b64":"GVhUPJQ7jvA45H+u04QZiB5pAtiivrx/rQrlatB8f9A2KHglw9AcVg4CBHWyiUw5xMjVdvsDpLjwXXy92cH6Cw==","signed_message":"canonical_sha256_bytes","builder_version":"pith-number-builder-2026-05-17-v1","receipt_version":"0.3","canonical_sha256":"4bab5777944f07600932df4a44682fd3396f12b3bfb22b4196c884fbfbbe2b6e","last_reissued_at":"2026-07-05T01:06:15.529113Z","signature_status":"signed_v1","first_computed_at":"2026-07-05T01:06:15.529113Z","public_key_fingerprint":"8d4b5ee74e4693bcd1df2446408b0d54"},"graph_snapshot":{"paper":{"title":"Inhibiting amyloid-like aggregation through bio-conjugation of proteins with polymer surfactant","license":"http://creativecommons.org/licenses/by/4.0/","headline":"","cross_cats":["cond-mat.soft","physics.bio-ph"],"primary_cat":"q-bio.BM","authors_text":"Anasua Mukhopadhyay, David A. King, Erika Eiser, Iliya D. Stoev, Kamendra P. Sharma","submitted_at":"2020-05-27T14:42:09Z","abstract_excerpt":"Prevention of protein aggregation and thus stabilization of proteins has large biological and biotechnological implications. Here, we show that inhibition of amyloid-like aggregates is possible in stoichiometric conjugates of polymer surfactant and bovine serum albumin (BSA) chosen as a model protein. We investigate using a combination of Thioflavin-T fluorescence spectroscopy, dynamic light scattering and FTIR spectroscopy the aggregation behavior in polymer surfactant modified and unmodified (native) BSA solutions. The BSA-polymer surfactant conjugates are stable up to 5 days under aggregati"},"claims":{"count":0,"items":[],"snapshot_sha256":"258153158e38e3291e3d48162225fcdb2d5a3ed65a07baac614ab91432fd4f57"},"source":{"id":"2005.13389","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/2005.13389/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":"2005.13389","created_at":"2026-07-05T01:06:15.529170+00:00"},{"alias_kind":"arxiv_version","alias_value":"2005.13389v1","created_at":"2026-07-05T01:06:15.529170+00:00"},{"alias_kind":"doi","alias_value":"10.48550/arxiv.2005.13389","created_at":"2026-07-05T01:06:15.529170+00:00"},{"alias_kind":"pith_short_12","alias_value":"JOVVO54UJ4DW","created_at":"2026-07-05T01:06:15.529170+00:00"},{"alias_kind":"pith_short_16","alias_value":"JOVVO54UJ4DWACJS","created_at":"2026-07-05T01:06:15.529170+00:00"},{"alias_kind":"pith_short_8","alias_value":"JOVVO54U","created_at":"2026-07-05T01:06:15.529170+00:00"}],"events":[],"event_summary":{},"paper_claims":[],"inbound_citations":{"count":0,"internal_anchor_count":0,"sample":[]},"formal_canon":{"evidence_count":0,"sample":[],"anchors":[]},"links":{"html":"https://pith.science/pith/JOVVO54UJ4DWACJS35FEI2BP2M","json":"https://pith.science/pith/JOVVO54UJ4DWACJS35FEI2BP2M.json","graph_json":"https://pith.science/api/pith-number/JOVVO54UJ4DWACJS35FEI2BP2M/graph.json","events_json":"https://pith.science/api/pith-number/JOVVO54UJ4DWACJS35FEI2BP2M/events.json","paper":"https://pith.science/paper/JOVVO54U"},"agent_actions":{"view_html":"https://pith.science/pith/JOVVO54UJ4DWACJS35FEI2BP2M","download_json":"https://pith.science/pith/JOVVO54UJ4DWACJS35FEI2BP2M.json","view_paper":"https://pith.science/paper/JOVVO54U","resolve_alias":"https://pith.science/api/pith-number/resolve?arxiv=2005.13389&json=true","fetch_graph":"https://pith.science/api/pith-number/JOVVO54UJ4DWACJS35FEI2BP2M/graph.json","fetch_events":"https://pith.science/api/pith-number/JOVVO54UJ4DWACJS35FEI2BP2M/events.json","actions":{"anchor_timestamp":"https://pith.science/pith/JOVVO54UJ4DWACJS35FEI2BP2M/action/timestamp_anchor","attest_storage":"https://pith.science/pith/JOVVO54UJ4DWACJS35FEI2BP2M/action/storage_attestation","attest_author":"https://pith.science/pith/JOVVO54UJ4DWACJS35FEI2BP2M/action/author_attestation","sign_citation":"https://pith.science/pith/JOVVO54UJ4DWACJS35FEI2BP2M/action/citation_signature","submit_replication":"https://pith.science/pith/JOVVO54UJ4DWACJS35FEI2BP2M/action/replication_record"}},"created_at":"2026-07-05T01:06:15.529170+00:00","updated_at":"2026-07-05T01:06:15.529170+00:00"}