{"doi":"10.1021/jacs.5c05344","title":"Sequence Programmable Order–Disorder Transitions in Supramolecular Assembly of Peptide Nanofibers","abstract":null,"journal":"Journal of the American Chemical Society","year":2025,"id":605197,"datarank":0.20794415416798362,"base_score":1.3862943611198906,"endowment":1.3862943611198906,"self_citation_contribution":0.20794415416798362,"citation_network_contribution":0.0,"self_endowment_contribution":0.20794415416798362,"citer_contribution":0.0,"corpus_percentile":null,"corpus_rank":null,"citation_count":3,"citer_count":0,"citers_with_citation_signal":0,"citers_with_endowment":0,"datacite_reuse_total":0,"is_dataset":false,"is_dataset_confidence":null,"is_data_producer":false,"deposit_databanks":null,"is_oa":false,"file_count":0,"downloads":0,"has_version_chain":false,"published_date":null,"fair_score":null,"fair_percentile":null,"algorithm_id":"datarank_citation_only_1hop_v6","ranking_scope":"data_only","authors":[{"id":433520,"name":"Naomy Marrufo","orcid":"0000-0003-1458-6594","position":1,"is_corresponding":false},{"id":1553114,"name":"Quynh Theresa H. Do","orcid":null,"position":2,"is_corresponding":false},{"id":1553115,"name":"Jully Nguyen Le","orcid":null,"position":3,"is_corresponding":false},{"id":735333,"name":"Michał Wierzbicki","orcid":"0000-0002-9217-634X","position":4,"is_corresponding":false},{"id":1553116,"name":"Yuanming Song","orcid":null,"position":5,"is_corresponding":false},{"id":469705,"name":"Khawla Mustafa","orcid":"0000-0001-8771-0571","position":6,"is_corresponding":false},{"id":305489,"name":"Fengbin Wang","orcid":"0000-0003-1008-663X","position":7,"is_corresponding":false},{"id":305492,"name":"Edward H. Egelman","orcid":"0000-0003-4844-5212","position":8,"is_corresponding":false},{"id":1553119,"name":"Zhibin Guan","orcid":"0000-0003-1370-1511","position":9,"is_corresponding":false},{"id":445432,"name":"Douglas J. Tobias","orcid":"0000-0002-6971-9828","position":10,"is_corresponding":false},{"id":260114,"name":"Allon I. Hochbaum","orcid":"0000-0002-5377-8065","position":11,"is_corresponding":false},{"id":1358327,"name":"Zachary J. Urbach","orcid":"0000-0003-0232-9662","position":0,"is_corresponding":false}],"reference_count":0,"raw_metadata":{"has_enrichment":true,"resolved":true,"title":"Sequence Programmable Order–Disorder Transitions in Supramolecular Assembly of Peptide Nanofibers","abstract":"Protein-protein interactions determine the assembly of complexes that are responsible for numerous key biological processes. The assembly of many natural protein complexes is mediated by post-translational structural changes and environmental stimuli. In this study, we show that incorporation of adjacent lysine residues results in the pH-tunable stability of peptide secondary structure and assembly, allowing for the incorporation of complementary order-inducing motifs. The strategic placement of cysteine pairs in the same peptide sequence results in redox-dependent disulfide staple formation, inducing a transition from random coil to β-sheet conformation and subsequent supramolecular nanofiber assembly from otherwise disordered peptide monomers. Spectroscopic, imaging, molecular dynamics, and kinetic studies highlight the critical role of sequence motif location, oligomerization, and the competitive interplay between intra- and interpeptide disulfide bonding in determining assembly outcomes. We extend this approach to demonstrate phosphorylation-dependent assembly from the design of the same parent peptide sequence, suggesting a general approach to the design of diverse stimulus-responsive peptide sequences for supramolecular assembly. These findings also provide a framework for investigating sequence-dependent pathways in amyloid fiber formation with potential implications for neurodegenerative disease research.","is_dataset_classified":null,"base_score":1.3862943611198906,"endowment":1.3862943611198906,"datacite_reuse_total":0,"file_count":0,"downloads":0,"views":0,"has_version_chain":false,"is_dataset":false,"is_oa":false,"pmid":"40622171","pmcid":"PMC12422407","openalex_id":"https://openalex.org/W4412088260","authors":[],"funders":[{"funder_name":"Air Force Office of Scientific Research","grant_id":"FA9550-19-1-0380","title":null},{"funder_name":"U.S. Department of Energy","grant_id":"DE-SC0020322","title":null},{"funder_name":"National Institute of General Medical Sciences","grant_id":"GM122510","title":null},{"funder_name":"Division of Materials Research","grant_id":"DMR-2011967","title":null},{"funder_name":"NIGMS NIH HHS","grant_id":"R35 GM122510","title":null}],"total_grants":5,"fwci":0.994,"citation_percentile":0.73459405,"influential_citations":0,"citation_trend":[{"year":2026,"count":3}],"oa_status":"green","license":"https://doi.org/10.15223/policy-029","oa_locations":[{"url":"https://pmc.ncbi.nlm.nih.gov/articles/PMC12422407/","host_type":"repository"},{"url":"https://pmc.ncbi.nlm.nih.gov/articles/PMC12422407/","host_type":"repository"},{"url":"https://pubs.acs.org/doi/pdf/10.1021/jacs.5c05344","host_type":"publisher"},{"url":"https://doi.org/10.1021/jacs.5c05344","host_type":"journal"},{"url":"https://pubmed.ncbi.nlm.nih.gov/40622171","host_type":"repository"}],"fields_of_study":["Supramolecular Self-Assembly in Materials","Chemical Synthesis and Analysis","Protein Structure and Dynamics","Nanofibers","Peptides","Molecular Dynamics Simulation","Amino Acid Sequence","Hydrogen-Ion Concentration","Protein Structure, Secondary"],"mesh_terms":["Amino Acid Sequence","Hydrogen-Ion Concentration","Peptides","Protein Structure, Secondary","Molecular Dynamics Simulation","Nanofibers"],"keywords":["Chemistry","Peptide","Supramolecular chemistry","Sequence (biology)","Peptide sequence","Biophysics","Nanofiber","Coiled coil","Random coil","Protein structure","Nanotechnology","Biochemistry","Protein secondary structure","Crystallography","Biology"],"sdg_mappings":[],"linked_datasets":[],"clinical_trials":[],"software_tools":[],"database_accessions":[],"source":"live","citation_network_status":"fetched"},"created_at":"2026-07-30T01:52:55.833466Z","pmid":null,"pmcid":null,"fwci":null,"citation_percentile":null,"influential_citations":0,"oa_status":null,"license":null,"views":0,"total_file_size_bytes":0,"version_count":0,"fair_f":null,"fair_a":null,"fair_i":null,"fair_r":null,"fair_zscore":null,"fair_rationale":null,"fair_model":null,"fair_agent_version":null,"fair_fulltext_source":null,"fair_has_llm":null,"fair_computed_at":null,"clinical_trials":[],"software_tools":[],"db_accessions":[],"linked_datasets":[],"topics":[]}