{"doi":"10.1016/j.actbio.2016.07.021","title":"Controlling gelation with sequence: Towards programmable peptide hydrogels","abstract":null,"journal":"Acta Biomaterialia","year":2016,"id":655236,"datarank":0.44166584687496613,"base_score":2.9444389791664403,"endowment":2.9444389791664403,"self_citation_contribution":0.44166584687496613,"citation_network_contribution":0.0,"self_endowment_contribution":0.44166584687496613,"citer_contribution":0.0,"corpus_percentile":null,"corpus_rank":null,"citation_count":18,"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":1710365,"name":"Bradley W. Mansel","orcid":null,"position":1,"is_corresponding":false},{"id":1710367,"name":"Martin A.K. Williams","orcid":null,"position":2,"is_corresponding":false},{"id":635185,"name":"Margaret A. Brimble","orcid":"0000-0002-7086-4096","position":3,"is_corresponding":false},{"id":533482,"name":"David E. Williams","orcid":"0000-0003-4627-8270","position":4,"is_corresponding":false},{"id":1662241,"name":"Juliet A. Gerrard","orcid":null,"position":5,"is_corresponding":false},{"id":1710363,"name":"Karima Medini","orcid":null,"position":0,"is_corresponding":false}],"reference_count":0,"raw_metadata":{"has_enrichment":true,"resolved":true,"title":"Controlling gelation with sequence: Towards programmable peptide hydrogels","abstract":"<h4>Unlabelled</h4>The self-assembling peptide IKHLSVN, inspired by inspection of a protein-protein interface, has previously been reported as one of a new class of bio-inspired peptides. Here the peptide, dubbed littleSven, and modifications designed to probe the resilience of the sequence to self-assembly, is characterised. Although the parent peptide did not form a hydrogel, small modifications to the sequence (one side chain or an N-terminus modification) led to hydrogels with properties (eg. gelation time and rheology) that could be tuned by these small alterations. The results suggest that peptides derived from protein-protein interfaces are resilient to changes in sequence and can be harnessed to form hydrogels with controlled properties.<h4>Statement of significance</h4>Natural occurring self-assembly peptides are attractive building blocks for engineered bionanomaterials due to their biocompatibility and biodegradability. The bio-inspired self-assembly peptide, IKHLSVN, was used as a template to design peptides that readily formed hydrogels. The peptide sequence was specifically tuned to create a bionanomaterial with different properties that could be exploited downstream for a broad range of applications: nanowires, drug release, vaccine adjuvant, tissue engineering. We describe how small modifications to the parent peptide alter the amyloid-like characteristics and gel strength for each peptide.","is_dataset_classified":null,"base_score":2.9444389791664403,"endowment":2.9444389791664403,"datacite_reuse_total":0,"file_count":0,"downloads":0,"views":0,"has_version_chain":false,"is_dataset":false,"is_oa":false,"pmid":"27424085","pmcid":null,"openalex_id":"https://openalex.org/W2469651751","authors":[],"funders":[],"total_grants":0,"fwci":0.9984,"citation_percentile":0.75206809,"influential_citations":0,"citation_trend":[{"year":2017,"count":4},{"year":2018,"count":1},{"year":2019,"count":1},{"year":2020,"count":3},{"year":2021,"count":2},{"year":2023,"count":2},{"year":2024,"count":4},{"year":2026,"count":1}],"oa_status":"green","license":"cc-by","oa_locations":[{"url":"https://hdl.handle.net/2292/32200","host_type":"repository"},{"url":"https://hdl.handle.net/2292/32200","host_type":"repository"},{"url":"https://api.elsevier.com/content/article/PII:S1742706116303476?httpAccept=text/xml","host_type":"publisher"},{"url":"https://api.elsevier.com/content/article/PII:S1742706116303476?httpAccept=text/plain","host_type":"publisher"},{"url":"https://doi.org/10.1016/j.actbio.2016.07.021","host_type":"journal"},{"url":"https://pubmed.ncbi.nlm.nih.gov/27424085","host_type":"repository"}],"fields_of_study":["Supramolecular Self-Assembly in Materials","Polydiacetylene-based materials and applications","Hydrogels: synthesis, properties, applications","Amino Acid Sequence","Hydrogels","Mechanical Phenomena","Nanofibers","Peptides","Spectroscopy, Fourier Transform Infrared","Spectrum Analysis","X-Ray Diffraction"],"mesh_terms":["Amino Acid Sequence","Peptides","Spectrum Analysis","X-Ray Diffraction","Spectroscopy, Fourier Transform Infrared","Hydrogels","Mechanical Phenomena","Nanofibers"],"keywords":["Self-healing hydrogels","Peptide","Materials science","Self-assembling peptide","Biocompatibility","Sequence (biology)","Peptide sequence","Biophysics","Nanotechnology","Self-assembly","Biochemistry","Chemistry","Biology","Polymer chemistry","hydrogels","Bionanomaterial","Amyloid-like Fibre","Diffusing Wave Spectroscopy"],"sdg_mappings":[],"linked_datasets":[],"clinical_trials":[],"software_tools":[],"database_accessions":[],"source":"live","citation_network_status":"fetched"},"created_at":"2026-08-11T10:10:43.336982Z","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":[]}