{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,11,5]],"date-time":"2026-11-05T22:34:20Z","timestamp":1793918060368,"version":"4.8.0"},"reference-count":148,"publisher":"Springer Science and Business Media LLC","issue":"8","license":[{"start":{"date-parts":[[2026,7,15]],"date-time":"2026-07-15T00:00:00Z","timestamp":1784073600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.springernature.com\/gp\/researchers\/text-and-data-mining"},{"start":{"date-parts":[[2026,7,15]],"date-time":"2026-07-15T00:00:00Z","timestamp":1784073600000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/www.springernature.com\/gp\/researchers\/text-and-data-mining"}],"content-domain":{"domain":["link.springer.com"],"crossmark-restriction":false},"short-container-title":["Nat Rev Chem"],"DOI":"10.1038\/s41570-026-00846-3","type":"journal-article","created":{"date-parts":[[2026,7,15]],"date-time":"2026-07-15T15:50:28Z","timestamp":1784130628000},"page":"558-576","update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":1,"title":["Bridging stimulus-responsive and dissipative peptide assemblies to build complex interactive biomaterials"],"prefix":"10.1038","volume":"10","author":[{"given":"Maximilian","family":"Schuler","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ayan","family":"Chatterjee","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-0302-0678","authenticated-orcid":false,"given":"David Y. W.","family":"Ng","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-5906-7205","authenticated-orcid":false,"given":"Tanja","family":"Weil","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"297","published-online":{"date-parts":[[2026,7,15]]},"reference":[{"key":"846_CR1","doi-asserted-by":"publisher","first-page":"582","DOI":"10.1002\/wnan.1238","volume":"5","author":"AC Mendes","year":"2013","unstructured":"Mendes, A. C., Baran, E. T., Reis, R. L. & Azevedo, H. S. Self-assembly in nature: using the principles of nature to create complex nanobiomaterials. Wiley Interdiscip. Rev. Nanomed. Nanobiotechnol. 5, 582\u2013612 (2013).","journal-title":"Wiley Interdiscip. Rev. Nanomed. Nanobiotechnol."},{"key":"846_CR2","doi-asserted-by":"publisher","first-page":"4739","DOI":"10.1016\/j.jmb.2016.09.022","volume":"428","author":"A Honigmann","year":"2016","unstructured":"Honigmann, A. & Pralle, A. Compartmentalization of the cell membrane. J. Mol. Biol. 428, 4739\u20134748 (2016).","journal-title":"J. Mol. Biol."},{"key":"846_CR3","doi-asserted-by":"publisher","first-page":"2344","DOI":"10.1039\/D4CS01095G","volume":"54","author":"A Cumberworth","year":"2025","unstructured":"Cumberworth, A. & Reinhardt, A. Models and simulations of structural DNA nanotechnology reveal fundamental principles of self-assembly. Chem. Soc. Rev. 54, 2344\u20132368 (2025).","journal-title":"Chem. Soc. Rev."},{"key":"846_CR4","doi-asserted-by":"publisher","first-page":"469","DOI":"10.1038\/nnano.2011.102","volume":"6","author":"TPJ Knowles","year":"2011","unstructured":"Knowles, T. P. J. & Buehler, M. J. Nanomechanics of functional and pathological amyloid materials. Nat. Nanotechnol. 6, 469\u2013479 (2011).","journal-title":"Nat. Nanotechnol."},{"key":"846_CR5","doi-asserted-by":"publisher","first-page":"476","DOI":"10.1016\/j.semcdb.2011.03.011","volume":"22","author":"KJ Wolfe","year":"2011","unstructured":"Wolfe, K. J. & Cyr, D. M. Amyloid in neurodegenerative diseases: friend or foe? Semin. Cell Dev. Biol. 22, 476\u2013481 (2011).","journal-title":"Semin. Cell Dev. Biol."},{"key":"846_CR6","doi-asserted-by":"publisher","first-page":"1230","DOI":"10.1126\/science.aba3526","volume":"367","author":"R Hervas","year":"2020","unstructured":"Hervas, R. et al. Cryo-EM structure of a neuronal functional amyloid implicated in memory persistence in Drosophila. Science 367, 1230\u20131234 (2020).","journal-title":"Science"},{"key":"846_CR7","doi-asserted-by":"publisher","first-page":"848","DOI":"10.1126\/science.abh3602","volume":"374","author":"Z \u00c1lvarez","year":"2021","unstructured":"\u00c1lvarez, Z. et al. Bioactive scaffolds with enhanced supramolecular motion promote recovery from spinal cord injury. Science 374, 848\u2013856 (2021).","journal-title":"Science"},{"key":"846_CR8","doi-asserted-by":"publisher","first-page":"45","DOI":"10.1016\/j.trechm.2022.11.003","volume":"5","author":"C Donau","year":"2023","unstructured":"Donau, C. & Boekhoven, J. The chemistry of chemically fueled droplets. Trends Chem. 5, 45\u201360 (2023).","journal-title":"Trends Chem."},{"key":"846_CR9","doi-asserted-by":"publisher","DOI":"10.1038\/s41467-023-44278-9","volume":"15","author":"S Cao","year":"2024","unstructured":"Cao, S. et al. Dipeptide coacervates as artificial membraneless organelles for bioorthogonal catalysis. Nat. Commun. 15, 39 (2024).","journal-title":"Nat. Commun."},{"key":"846_CR10","doi-asserted-by":"publisher","first-page":"2524","DOI":"10.1021\/acs.biomac.1c00267","volume":"22","author":"S Yamamoto","year":"2021","unstructured":"Yamamoto, S. et al. Microenvironment pH-induced selective cell death for potential cancer therapy using nanofibrous self-assembly of a peptide amphiphile. Biomacromolecules 22, 2524\u20132531 (2021).","journal-title":"Biomacromolecules"},{"key":"846_CR11","doi-asserted-by":"publisher","DOI":"10.1002\/adfm.201904969","volume":"30","author":"D-S Yang","year":"2020","unstructured":"Yang, D.-S. et al. A redox-triggered bispecific supramolecular nanomedicine based on peptide self-assembly for high-efficacy and low-toxic cancer therapy. Adv. Funct. Mater. 30, 1904969 (2020).","journal-title":"Adv. Funct. Mater."},{"key":"846_CR12","doi-asserted-by":"publisher","DOI":"10.1002\/advs.202515237","volume":"13","author":"X Yang","year":"2026","unstructured":"Yang, X. et al. Peptide sequence programmed piezoelectric response by supramolecular self-assembly. Adv. Sci. 13, e15237 (2026).","journal-title":"Adv. Sci."},{"key":"846_CR13","doi-asserted-by":"publisher","first-page":"10807","DOI":"10.1021\/acs.jmedchem.6b00319","volume":"59","author":"MAT Blaskovich","year":"2016","unstructured":"Blaskovich, M. A. T. Unusual amino acids in medicinal chemistry. J. Med. Chem. 59, 10807\u201310836 (2016).","journal-title":"J. Med. Chem."},{"key":"846_CR14","doi-asserted-by":"publisher","first-page":"94","DOI":"10.1016\/j.actbio.2022.05.012","volume":"146","author":"W Ye","year":"2022","unstructured":"Ye, W. et al. Articular cartilage reconstruction with TGF-\u03b21-simulating self-assembling peptide hydrogel-based composite scaffold. Acta Biomater. 146, 94\u2013106 (2022).","journal-title":"Acta Biomater."},{"key":"846_CR15","doi-asserted-by":"publisher","first-page":"15780","DOI":"10.1021\/jacs.0c05261","volume":"142","author":"M Pieszka","year":"2020","unstructured":"Pieszka, M. et al. Controlled supramolecular assembly inside living cells by sequential multistaged chemical reactions. J. Am. Chem. Soc. 142, 15780\u201315789 (2020).","journal-title":"J. Am. Chem. Soc."},{"key":"846_CR16","doi-asserted-by":"publisher","DOI":"10.1002\/adfm.202009382","volume":"31","author":"S Sieste","year":"2021","unstructured":"Sieste, S. et al. Supramolecular peptide nanofibrils with optimized sequences and molecular structures for efficient retroviral transduction. Adv. Funct. Mater. 31, 2009382 (2021).","journal-title":"Adv. Funct. Mater."},{"key":"846_CR17","volume":"33","author":"S Wu","year":"2021","unstructured":"Wu, S. et al. A mini-review on peptide-based self-assemblies and their biological applications. Nanotechnology 33, 062004 (2021).","journal-title":"Nanotechnology"},{"key":"846_CR18","doi-asserted-by":"publisher","first-page":"7483","DOI":"10.1039\/D0TB01147A","volume":"8","author":"SK Talloj","year":"2020","unstructured":"Talloj, S. K., Mohammed, M. & Lin, H. C. Construction of self-assembled nanostructure-based tetraphenylethylene dipeptides: supramolecular nanobelts as biomimetic hydrogels for cell adhesion and proliferation. J. Mater. Chem. B 8, 7483\u20137493 (2020).","journal-title":"J. Mater. Chem. B"},{"key":"846_CR19","doi-asserted-by":"publisher","DOI":"10.1002\/adma.202104704","volume":"34","author":"J Wang","year":"2022","unstructured":"Wang, J. et al. Intracellular condensates of oligopeptide for targeting lysosome and addressing multiple drug resistance of cancer. Adv. Mater. 34, e2104704 (2022).","journal-title":"Adv. Mater."},{"key":"846_CR20","doi-asserted-by":"publisher","DOI":"10.1002\/adma.201805044","volume":"31","author":"J Ga\u010danin","year":"2019","unstructured":"Ga\u010danin, J. et al. Autonomous ultrafast self-healing hydrogels by pH-responsive functional nanofiber gelators as cell matrices. Adv. Mater. 31, 1805044 (2019).","journal-title":"Adv. Mater."},{"key":"846_CR21","doi-asserted-by":"publisher","DOI":"10.1002\/anie.202212829","volume":"61","author":"H Dong","year":"2022","unstructured":"Dong, H. et al. Redox-regulated conformational change of disulfide-rich assembling peptides. Angew. Chem. Int. Ed. 61, e202212829 (2022).","journal-title":"Angew. Chem. Int. Ed."},{"key":"846_CR22","doi-asserted-by":"publisher","first-page":"9312","DOI":"10.1021\/jacs.2c01025","volume":"144","author":"X Liu","year":"2022","unstructured":"Liu, X. et al. In situ self-sorting peptide assemblies in living cells for simultaneous organelle targeting. J. Am. Chem. Soc. 144, 9312\u20139323 (2022).","journal-title":"J. Am. Chem. Soc."},{"key":"846_CR23","doi-asserted-by":"publisher","DOI":"10.1038\/s41467-019-09587-y","volume":"10","author":"AS Carlini","year":"2019","unstructured":"Carlini, A. S. et al. Enzyme-responsive progelator cyclic peptides for minimally invasive delivery to the heart post-myocardial infarction. Nat. Commun. 10, 1735 (2019).","journal-title":"Nat. Commun."},{"key":"846_CR24","doi-asserted-by":"publisher","DOI":"10.1038\/s41467-022-30634-8","volume":"13","author":"Y Zhou","year":"2022","unstructured":"Zhou, Y. et al. Peptide nano-blanket impedes fibroblasts activation and subsequent formation of pre-metastatic niche. Nat. Commun. 13, 2906 (2022).","journal-title":"Nat. Commun."},{"key":"846_CR25","doi-asserted-by":"publisher","first-page":"7800","DOI":"10.1021\/acsanm.1c01098","volume":"4","author":"E Olson","year":"2021","unstructured":"Olson, E. et al. Enzyme-instructed formation of \u03b2-sheet-rich nanoplatelets for label-free protease sensing. ACS Appl. Nano Mater. 4, 7800\u20137810 (2021).","journal-title":"ACS Appl. Nano Mater."},{"key":"846_CR26","doi-asserted-by":"publisher","DOI":"10.1002\/ADVS.202304164","author":"S Tanwar","year":"2023","unstructured":"Tanwar, S. et al. A smart intracellular self-assembling bioorthogonal Raman active nanoprobe for targeted tumor imaging. Adv. Sci. https:\/\/doi.org\/10.1002\/ADVS.202304164 (2023).","journal-title":"Adv. Sci."},{"key":"846_CR27","doi-asserted-by":"publisher","DOI":"10.1002\/anie.202214394","volume":"62","author":"Z Jin","year":"2023","unstructured":"Jin, Z. et al. Peptide amphiphile mediated co-assembly for nanoplasmonic sensing. Angew. Chem. Int. Ed. 62, e202214394 (2023).","journal-title":"Angew. Chem. Int. Ed."},{"key":"846_CR28","doi-asserted-by":"publisher","first-page":"12796","DOI":"10.1002\/anie.202102601","volume":"60","author":"W Tan","year":"2021","unstructured":"Tan, W. et al. Enzymatic assemblies of thiophosphopeptides instantly target Golgi apparatus and selectively kill cancer cells. Angew. Chem. Int. Ed. 60, 12796\u201312801 (2021).","journal-title":"Angew. Chem. Int. Ed."},{"key":"846_CR29","doi-asserted-by":"publisher","first-page":"26994","DOI":"10.1002\/anie.202110512","volume":"60","author":"S Ji","year":"2021","unstructured":"Ji, S. et al. Targeted enrichment of enzyme-instructed assemblies in cancer cell lysosomes turns immunologically cold tumors hot. Angew. Chem. Int. Ed. 60, 26994\u201327004 (2021).","journal-title":"Angew. Chem. Int. Ed."},{"key":"846_CR30","doi-asserted-by":"publisher","first-page":"18244","DOI":"10.1021\/acsnano.2c05825","volume":"16","author":"X Yang","year":"2022","unstructured":"Yang, X., Lu, H., Wu, B. & Wang, H. Triggered self-sorting of peptides to form higher-order assemblies in a living system. ACS Nano 16, 18244\u201318252 (2022).","journal-title":"ACS Nano"},{"key":"846_CR31","doi-asserted-by":"publisher","first-page":"8121","DOI":"10.1002\/anie.202014278","volume":"60","author":"Y Zhong","year":"2021","unstructured":"Zhong, Y. et al. Enzyme-instructed self-assembly enabled monomer\u2013excimer transition to construct higher ordered luminescent supramolecular assembly for activity-based bioimaging. Angew. Chem. Int. Ed. 60, 8121\u20138129 (2021).","journal-title":"Angew. Chem. Int. Ed."},{"key":"846_CR32","doi-asserted-by":"publisher","first-page":"5562","DOI":"10.1021\/jacs.2c00433","volume":"144","author":"R Qiu","year":"2022","unstructured":"Qiu, R. et al. Supramolecular copolymers of peptides and lipidated peptides and their therapeutic potential. J. Am. Chem. Soc. 144, 5562\u20135574 (2022).","journal-title":"J. Am. Chem. Soc."},{"key":"846_CR33","doi-asserted-by":"publisher","first-page":"3559","DOI":"10.1002\/cmdc.202100440","volume":"16","author":"R Feng","year":"2021","unstructured":"Feng, R. et al. Altered peptide self-assembly and co-assembly with DNA by modification of aromatic residues. ChemMedChem 16, 3559\u20133564 (2021).","journal-title":"ChemMedChem"},{"key":"846_CR34","doi-asserted-by":"publisher","first-page":"3578","DOI":"10.1002\/anie.201913611","volume":"59","author":"R Ni","year":"2020","unstructured":"Ni, R. & Chau, Y. Nanoassembly of oligopeptides and DNA mimics the sequential disassembly of a spherical virus. Angew. Chem. Int. Ed. 59, 3578\u20133584 (2020).","journal-title":"Angew. Chem. Int. Ed."},{"key":"846_CR35","doi-asserted-by":"publisher","first-page":"4837","DOI":"10.1166\/jnn.2014.8275","volume":"14","author":"H Liu","year":"2014","unstructured":"Liu, H., Song, Z. & Chen, X. Photo-controllable molecular hydrogels for drug delivery. J. Nanosci. Nanotechnol. 14, 4837\u20134842 (2014).","journal-title":"J. Nanosci. Nanotechnol."},{"key":"846_CR36","doi-asserted-by":"publisher","first-page":"5536","DOI":"10.1021\/acsnano.2c10896","volume":"17","author":"Y Xiang","year":"2023","unstructured":"Xiang, Y. et al. A facile and versatile approach to construct photoactivated peptide hydrogels by regulating electrostatic repulsion. ACS Nano 17, 5536\u20135547 (2023).","journal-title":"ACS Nano"},{"key":"846_CR37","doi-asserted-by":"publisher","DOI":"10.1002\/mabi.202200294","volume":"23","author":"K Kaygisiz","year":"2023","unstructured":"Kaygisiz, K. et al. Photoinduced amyloid fibril degradation for controlled cell patterning. Macromol. Biosci. 23, 2200294 (2023). This article shows how self-assembled peptides can be disassembled by means of a photosensitive linker to selectively promote cell adhesion on surfaces using photopatterning techniques.","journal-title":"Macromol. Biosci."},{"key":"846_CR38","doi-asserted-by":"publisher","DOI":"10.1038\/s41467-018-04488-y","volume":"9","author":"M Tena-Solsona","year":"2018","unstructured":"Tena-Solsona, M., Wanzke, C., Riess, B., Bausch, A. R. & Boekhoven, J. Self-selection of dissipative assemblies driven by primitive chemical reaction networks. Nat. Commun. 9, 2044 (2018).","journal-title":"Nat. Commun."},{"key":"846_CR39","doi-asserted-by":"publisher","DOI":"10.1038\/s41467-023-42344-w","volume":"14","author":"AM Bergmann","year":"2023","unstructured":"Bergmann, A. M. et al. Liquid spherical shells are a non-equilibrium steady state of active droplets. Nat. Commun. 14, 6552 (2023).","journal-title":"Nat. Commun."},{"key":"846_CR40","doi-asserted-by":"publisher","DOI":"10.1016\/j.chempr.2025.102578","volume":"11","author":"M Wenisch","year":"2025","unstructured":"Wenisch, M. et al. Toward synthetic life \u2014 emergence, growth, creation of offspring, decay, and rescue of fuel-dependent synthetic cells. Chem 11, 102578 (2025).","journal-title":"Chem"},{"key":"846_CR41","doi-asserted-by":"publisher","first-page":"29621","DOI":"10.1021\/jacs.4c10082","volume":"146","author":"MD Pol","year":"2024","unstructured":"Pol, M. D., Thomann, R., Thomann, Y. & Pappas, C. G. Abiotic acyl transfer cascades driven by aminoacyl phosphate esters and self-assembly. J. Am. Chem. Soc. 146, 29621\u201329629 (2024). This article describes cascade reactions in chemical rection networks driven by abiotic phosphate esters.","journal-title":"J. Am. Chem. Soc."},{"key":"846_CR42","doi-asserted-by":"publisher","DOI":"10.1002\/anie.202404360","volume":"63","author":"MD Pol","year":"2024","unstructured":"Pol, M. D. et al. Guiding transient peptide assemblies with structural elements embedded in abiotic phosphate fuels. Angew. Chem. Int. Ed. 63, e202404360 (2024).","journal-title":"Angew. Chem. Int. Ed."},{"key":"846_CR43","doi-asserted-by":"publisher","first-page":"8372","DOI":"10.1002\/chem.202001008","volume":"26","author":"M Kumar","year":"2020","unstructured":"Kumar, M., Sementa, D., Narang, V., Riedo, E. & Ulijn, R. V. Self-assembly propensity dictates lifetimes in transient naphthalimide\u2013dipeptide nanofibers. Chem. Eur. J. 26, 8372\u20138376 (2020).","journal-title":"Chem. Eur. J."},{"key":"846_CR44","doi-asserted-by":"publisher","first-page":"696","DOI":"10.1038\/s41557-018-0047-2","volume":"10","author":"M Kumar","year":"2018","unstructured":"Kumar, M. et al. Amino-acid-encoded biocatalytic self-assembly enables the formation of transient conducting nanostructures. Nat. Chem. 10, 696\u2013703 (2018).","journal-title":"Nat. Chem."},{"key":"846_CR45","doi-asserted-by":"publisher","first-page":"14674","DOI":"10.1039\/D1SC03492H","volume":"12","author":"SP Afrose","year":"2021","unstructured":"Afrose, S. P., Ghosh, C. & Das, D. Substrate induced generation of transient self-assembled catalytic systems. Chem. Sci. 12, 14674\u201314685 (2021).","journal-title":"Chem. Sci."},{"key":"846_CR46","doi-asserted-by":"publisher","DOI":"10.3390\/biom11020336","volume":"11","author":"R Melchionna","year":"2021","unstructured":"Melchionna, R., Trono, P., Tocci, A. & Nistic\u00f2, P. Actin cytoskeleton and regulation of TGF\u03b2 signaling: exploring their links. Biomolecules 11, 336 (2021).","journal-title":"Biomolecules"},{"key":"846_CR47","doi-asserted-by":"publisher","first-page":"5519","DOI":"10.1039\/C7CS00246G","volume":"46","author":"SAP Van Rossum","year":"2017","unstructured":"Van Rossum, S. A. P., Tena-Solsona, M., Van Esch, J. H., Eelkema, R. & Boekhoven, J. Dissipative out-of-equilibrium assembly of man-made supramolecular materials. Chem. Soc. Rev. 46, 5519\u20135535 (2017).","journal-title":"Chem. Soc. Rev."},{"key":"846_CR48","doi-asserted-by":"publisher","first-page":"14142","DOI":"10.1021\/jacs.0c04203","volume":"142","author":"K Dai","year":"2020","unstructured":"Dai, K. et al. Regulating chemically fueled peptide assemblies by molecular design. J. Am. Chem. Soc. 142, 14142\u201314149 (2020).","journal-title":"J. Am. Chem. Soc."},{"key":"846_CR49","doi-asserted-by":"publisher","DOI":"10.1038\/s43246-021-00202-6","volume":"2","author":"M Kretschmer","year":"2021","unstructured":"Kretschmer, M., Winkeljann, B., Kriebisch, B. A. K., Boekhoven, J. & Lieleg, O. Viscoelastic behavior of chemically fueled supramolecular hydrogels under load and influence of reaction side products. Commun. Mater. 2, 97 (2021).","journal-title":"Commun. Mater."},{"key":"846_CR50","doi-asserted-by":"publisher","DOI":"10.1038\/s41467-020-18815-9","volume":"11","author":"C Donau","year":"2020","unstructured":"Donau, C. et al. Active coacervate droplets as a model for membraneless organelles and protocells. Nat. Commun. 11, 5167 (2020).","journal-title":"Nat. Commun."},{"key":"846_CR51","doi-asserted-by":"publisher","DOI":"10.1038\/ncomms15899","volume":"8","author":"A Sorrenti","year":"2017","unstructured":"Sorrenti, A., Leira-Iglesias, J., Sato, A. & Hermans, T. M. Non-equilibrium steady states in supramolecular polymerization. Nat. Commun. 8, 15899 (2017).","journal-title":"Nat. Commun."},{"key":"846_CR52","doi-asserted-by":"publisher","DOI":"10.1038\/s41467-024-48571-z","volume":"15","author":"SM Poprawa","year":"2024","unstructured":"Poprawa, S. M. et al. Active droplets through enzyme-free, dynamic phosphorylation. Nat. Commun. 15, 4204 (2024).","journal-title":"Nat. Commun."},{"key":"846_CR53","doi-asserted-by":"publisher","first-page":"8119","DOI":"10.1002\/anie.201500867","volume":"54","author":"CG Pappas","year":"2015","unstructured":"Pappas, C. G., Sasselli, I. R. & Ulijn, R. V. Biocatalytic pathway selection in transient tripeptide nanostructures. Angew. Chem. Int. Ed. 54, 8119\u20138123 (2015).","journal-title":"Angew. Chem. Int. Ed."},{"key":"846_CR54","doi-asserted-by":"publisher","DOI":"10.1002\/chem.202203820","volume":"29","author":"S Chowdhuri","year":"2023","unstructured":"Chowdhuri, S. et al. Cumulative effect of pH and redox triggers on highly adaptive transient coacervates. Chem. Eur. J. 29, e202203820 (2023). This article demonstrates a transient amino acid\/polymer-based coacervation system that can be tuned by pH and redox profiles.","journal-title":"Chem. Eur. J."},{"key":"846_CR55","doi-asserted-by":"publisher","first-page":"244","DOI":"10.1002\/anie.201811749","volume":"58","author":"S Bal","year":"2019","unstructured":"Bal, S., Das, K., Ahmed, S. & Das, D. Chemically fueled dissipative self-assembly that exploits cooperative catalysis. Angew. Chem. Int. Ed. 58, 244\u2013247 (2019).","journal-title":"Angew. Chem. Int. Ed."},{"key":"846_CR56","doi-asserted-by":"publisher","first-page":"15783","DOI":"10.1002\/anie.201910280","volume":"58","author":"SP Afrose","year":"2019","unstructured":"Afrose, S. P., Bal, S., Chatterjee, A., Das, K. & Das, D. Designed negative feedback from transiently formed catalytic nanostructures. Angew. Chem. Int. Ed. 58, 15783\u201315787 (2019).","journal-title":"Angew. Chem. Int. Ed."},{"key":"846_CR57","doi-asserted-by":"publisher","DOI":"10.1002\/anie.202511352","volume":"65","author":"A Chatterjee","year":"2026","unstructured":"Chatterjee, A. et al. Regulating promiscuous catalysis via substrate-induced transient assembly. Angew. Chem. Int. Ed. 65, e202511352 (2026). This article describes a transient catalytically active hydrogel that exhibits catalytic promiscuity and self-degradation.","journal-title":"Angew. Chem. Int. Ed."},{"key":"846_CR58","doi-asserted-by":"publisher","first-page":"13776","DOI":"10.1039\/D1CC04971B","volume":"57","author":"M Liu","year":"2021","unstructured":"Liu, M. et al. Light-driven dissipative self-assembly of a peptide hydrogel. Chem. Commun. 57, 13776\u201313779 (2021).","journal-title":"Chem. Commun."},{"key":"846_CR59","doi-asserted-by":"publisher","DOI":"10.1002\/syst.202000012","volume":"2","author":"N Ciss\u00e9","year":"2020","unstructured":"Ciss\u00e9, N. & Kudernac, T. Light-fuelled self-assembly of cyclic peptides into supramolecular tubules. ChemSystemsChem 2, e2000012 (2020).","journal-title":"ChemSystemsChem"},{"key":"846_CR60","doi-asserted-by":"publisher","DOI":"10.1038\/ncomms15895","volume":"8","author":"M Tena-Solsona","year":"2017","unstructured":"Tena-Solsona, M. et al. Non-equilibrium dissipative supramolecular materials with a tunable lifetime. Nat. Commun. 8, 15895 (2017).","journal-title":"Nat. Commun."},{"key":"846_CR61","doi-asserted-by":"publisher","DOI":"10.3390\/ijms20235850","volume":"20","author":"S Lee","year":"2019","unstructured":"Lee, S. et al. Self-assembling peptides and their application in the treatment of diseases. Int. J. Mol. Sci. 20, 5850 (2019).","journal-title":"Int. J. Mol. Sci."},{"key":"846_CR62","doi-asserted-by":"publisher","first-page":"320","DOI":"10.1038\/s41570-022-00373-x","volume":"6","author":"S Chagri","year":"2022","unstructured":"Chagri, S., Ng, D. Y. W. & Weil, T. Designing bioresponsive nanomaterials for intracellular self-assembly. Nat. Rev. Chem. 6, 320\u2013338 (2022).","journal-title":"Nat. Rev. Chem."},{"key":"846_CR63","doi-asserted-by":"publisher","first-page":"1999","DOI":"10.1021\/acs.molpharmaceut.1c00983","volume":"19","author":"V Devika","year":"2022","unstructured":"Devika, V. et al. Recent advances in peptides-based stimuli-responsive materials for biomedical and therapeutic applications: a review. Mol. Pharm. 19, 1999\u20132021 (2022).","journal-title":"Mol. Pharm."},{"key":"846_CR64","doi-asserted-by":"publisher","DOI":"10.1002\/agt2.110","volume":"2","author":"Q Wang","year":"2021","unstructured":"Wang, Q., Qi, Z., Chen, M. & Qu, D. H. Out-of-equilibrium supramolecular self-assembling systems driven by chemical fuel. Aggregate 2, e110 (2021).","journal-title":"Aggregate"},{"key":"846_CR65","doi-asserted-by":"publisher","first-page":"5476","DOI":"10.1039\/C7CS00121E","volume":"46","author":"A Sorrenti","year":"2017","unstructured":"Sorrenti, A., Leira-Iglesias, J., Markvoort, A. J., De Greef, T. F. A. & Hermans, T. M. Non-equilibrium supramolecular polymerization. Chem. Soc. Rev. 46, 5476\u20135490 (2017).","journal-title":"Chem. Soc. Rev."},{"key":"846_CR66","doi-asserted-by":"publisher","first-page":"416","DOI":"10.1021\/accountsmr.2c00244","volume":"4","author":"X Chen","year":"2023","unstructured":"Chen, X., W\u00fcrbser, M. A. & Boekhoven, J. Chemically fueled supramolecular materials. Acc. Mater. Res. 4, 416\u2013426 (2023).","journal-title":"Acc. Mater. Res."},{"key":"846_CR67","doi-asserted-by":"publisher","first-page":"19932","DOI":"10.1021\/acs.jmedchem.4c00110","volume":"67","author":"KK Sharma","year":"2024","unstructured":"Sharma, K. K. et al. Unnatural amino acids: strategies, designs, and applications in medicinal chemistry and drug discovery. J. Med. Chem. 67, 19932\u201319965 (2024).","journal-title":"J. Med. Chem."},{"key":"846_CR68","doi-asserted-by":"publisher","first-page":"8176","DOI":"10.1021\/acs.jpcb.3c05598","volume":"127","author":"Y Li","year":"2023","unstructured":"Li, Y. et al. Aggregation-induced asymmetric charge states of amino acids in supramolecular nanofibers. J. Phys. Chem. B 127, 8176\u20138184 (2023).","journal-title":"J. Phys. Chem. B"},{"key":"846_CR69","doi-asserted-by":"publisher","DOI":"10.1002\/anie.202201791","volume":"61","author":"BP Nowak","year":"2022","unstructured":"Nowak, B. P., Schlichter, L. & Ravoo, B. J. Mediating oxidation of thioethers with iodine \u2014 a mild and versatile pathway to trigger the formation of peptide hydrogels. Angew. Chem. Int. Ed. 61, e202201791 (2022). This article shows a new approach to hydrogel formation using the oxidation of thioether with triiodide.","journal-title":"Angew. Chem. Int. Ed."},{"key":"846_CR70","doi-asserted-by":"publisher","first-page":"1317","DOI":"10.1021\/acs.jpcb.0c07713","volume":"125","author":"HC Fry","year":"2021","unstructured":"Fry, H. C., Peters, B. L. & Ferguson, A. L. Pushing and pulling: a dual pH trigger controlled by varying the alkyl tail length in heme coordinating peptide amphiphiles. J. Phys. Chem. B 125, 1317\u20131330 (2021).","journal-title":"J. Phys. Chem. B"},{"key":"846_CR71","doi-asserted-by":"publisher","first-page":"343","DOI":"10.1002\/cbf.1149","volume":"22","author":"GK Balendiran","year":"2004","unstructured":"Balendiran, G. K., Dabur, R. & Fraser, D. The role of glutathione in cancer. Cell Biochem. Funct. 22, 343\u2013352 (2004).","journal-title":"Cell Biochem. Funct."},{"key":"846_CR72","doi-asserted-by":"publisher","first-page":"1900","DOI":"10.1126\/science.1150057","volume":"318","author":"TP Knowles","year":"2007","unstructured":"Knowles, T. P. et al. Role of intermolecular forces in defining material properties of protein nanofibrils. Science 318, 1900\u20131903 (2007).","journal-title":"Science"},{"key":"846_CR73","doi-asserted-by":"publisher","first-page":"7965","DOI":"10.1021\/acs.nanolett.9b03136","volume":"19","author":"M Li","year":"2019","unstructured":"Li, M. et al. Proline isomerization-regulated tumor microenvironment-adaptable self-assembly of peptides for enhanced therapeutic efficacy. Nano Lett. 19, 7965\u20137976 (2019).","journal-title":"Nano Lett."},{"key":"846_CR74","doi-asserted-by":"publisher","first-page":"2444","DOI":"10.1039\/C8TB00448J","volume":"6","author":"Y Zhao","year":"2018","unstructured":"Zhao, Y. et al. A supramolecular approach to construct a hydrolase mimic with photo-switchable catalytic activity. J. Mater. Chem. B 6, 2444\u20132449 (2018).","journal-title":"J. Mater. Chem. B"},{"key":"846_CR75","doi-asserted-by":"publisher","first-page":"8171","DOI":"10.1039\/C9SC00193J","volume":"10","author":"L Chen","year":"2019","unstructured":"Chen, L. et al. Sequence isomerism-dependent self-assembly of glycopeptide mimetics with switchable antibiofilm properties. Chem. Sci. 10, 8171\u20138178 (2019).","journal-title":"Chem. Sci."},{"key":"846_CR76","doi-asserted-by":"publisher","first-page":"7299","DOI":"10.1039\/D0SM00835D","volume":"16","author":"BP Nowak","year":"2020","unstructured":"Nowak, B. P. & Ravoo, B. J. Photoresponsive hybrid hydrogel with a dual network of agarose and a self-assembling peptide. Soft Matter 16, 7299\u20137304 (2020).","journal-title":"Soft Matter"},{"key":"846_CR77","doi-asserted-by":"publisher","first-page":"220","DOI":"10.1039\/C9FD00012G","volume":"219","author":"BP Nowak","year":"2019","unstructured":"Nowak, B. P. & Ravoo, B. J. Magneto- and photo-responsive hydrogels from the co-assembly of peptides, cyclodextrins, and superparamagnetic nanoparticles. Faraday Discuss. 219, 220\u2013228 (2019).","journal-title":"Faraday Discuss."},{"key":"846_CR78","doi-asserted-by":"publisher","DOI":"10.3389\/fmolb.2023.1137885","volume":"10","author":"Y Liang","year":"2023","unstructured":"Liang, Y., Ogawa, S., Inaba, H. & Matsuura, K. Dramatic morphological changes in liposomes induced by peptide nanofibers reversibly polymerized and depolymerized by the photoisomerization of spiropyran. Front. Mol. Biosci. 10, 1137885 (2023).","journal-title":"Front. Mol. Biosci."},{"key":"846_CR79","doi-asserted-by":"publisher","DOI":"10.1002\/anie.202514781","volume":"65","author":"J Link","year":"2025","unstructured":"Link, J. et al. Photoswitchable peptides as molecular tools to encode structural order and disorder in intracellular assemblies. Angew. Chem. Int. Ed. 65, e14781 (2025).","journal-title":"Angew. Chem. Int. Ed."},{"key":"846_CR80","doi-asserted-by":"publisher","DOI":"10.3389\/fmolb.2022.896099","volume":"9","author":"S Mustafa","year":"2022","unstructured":"Mustafa, S., Koran, S. & AlOmair, L. Insights into the role of matrix metalloproteinases in cancer and its various therapeutic aspects: a review. Front. Mol. Biosci. 9, 896099 (2022).","journal-title":"Front. Mol. Biosci."},{"key":"846_CR81","doi-asserted-by":"publisher","DOI":"10.1002\/anie.202504958","volume":"64","author":"Y Li","year":"2025","unstructured":"Li, Y., Xu, T., Li, Y. & Wang, H. Enzyme induced solid-like condensates formation of engineered peptide in living cells for prostate cancer inhibition. Angew. Chem. Int. Ed. 64, e202504958 (2025).","journal-title":"Angew. Chem. Int. Ed."},{"key":"846_CR82","doi-asserted-by":"publisher","first-page":"4366","DOI":"10.1021\/jacs.2c11823","volume":"145","author":"Y Ding","year":"2023","unstructured":"Ding, Y. et al. Enzyme-instructed peptide assembly favored by preorganization for cancer cell membrane engineering. J. Am. Chem. Soc. 145, 4366\u20134371 (2023).","journal-title":"J. Am. Chem. Soc."},{"key":"846_CR83","doi-asserted-by":"publisher","first-page":"196","DOI":"10.1016\/j.msec.2017.03.103","volume":"76","author":"C Wu","year":"2017","unstructured":"Wu, C. et al. Redox-responsive supramolecular hydrogel based on 10-hydroxy camptothecin\u2013peptide covalent conjugates with high loading capacity for drug delivery. Mater. Sci. Eng. C 76, 196\u2013202 (2017).","journal-title":"Mater. Sci. Eng. C"},{"key":"846_CR84","volume":"8","author":"Z Wang","year":"2020","unstructured":"Wang, Z. et al. Co-assembled supramolecular nanofibers with tunable surface properties for efficient vaccine delivery. Front. Chem. 8, 548028 (2020).","journal-title":"Front. Chem."},{"key":"846_CR85","doi-asserted-by":"publisher","first-page":"57","DOI":"10.1021\/acsami.2c14413","volume":"15","author":"W Song","year":"2022","unstructured":"Song, W. et al. Enhancing photothermal therapy efficacy by in situ self-assembly in glioma. ACS Appl. Mater. Interfaces 15, 57\u201366 (2022).","journal-title":"ACS Appl. Mater. Interfaces"},{"key":"846_CR86","doi-asserted-by":"publisher","DOI":"10.1002\/adfm.202007733","volume":"31","author":"AS Carlini","year":"2021","unstructured":"Carlini, A. S., Choi, W., McCallum, N. C. & Gianneschi, N. C. pH-responsive charge-conversion progelator peptides. Adv. Funct. Mater. 31, 2007733 (2021).","journal-title":"Adv. Funct. Mater."},{"key":"846_CR87","doi-asserted-by":"publisher","first-page":"43","DOI":"10.1021\/mz500677q","volume":"4","author":"JB Matson","year":"2015","unstructured":"Matson, J. B., Navon, Y., Bitton, R. & Stupp, S. I. Light-controlled hierarchical self-assembly of polyelectrolytes and supramolecular polymers. ACS Macro Lett. 4, 43\u201347 (2015).","journal-title":"ACS Macro Lett."},{"key":"846_CR88","doi-asserted-by":"publisher","first-page":"2037","DOI":"10.1021\/jacs.4c15644","volume":"147","author":"SY Dai","year":"2025","unstructured":"Dai, S. Y., Xiao, Z., Shen, F., Lim, I. & Rao, J. Light-controlled intracellular synthesis of poly(luciferin) polymers induces cell paraptosis. J. Am. Chem. Soc. 147, 2037\u20132048 (2025).","journal-title":"J. Am. Chem. Soc."},{"key":"846_CR89","doi-asserted-by":"publisher","first-page":"980","DOI":"10.1038\/s44160-023-00343-1","volume":"2","author":"P Roth","year":"2023","unstructured":"Roth, P. et al. Supramolecular assembly guided by photolytic redox cycling. Nat. Synth. 2, 980\u2013988 (2023). This article describes a photolabile caging group with productive side reaction that affects self-assembly behaviour in a pathway-dependent manner.","journal-title":"Nat. Synth."},{"key":"846_CR90","doi-asserted-by":"publisher","first-page":"673","DOI":"10.1038\/s44160-025-00751-5","volume":"4","author":"Y Ren","year":"2025","unstructured":"Ren, Y. et al. Intracellular assembly of supramolecular peptide nanostructures controlled by visible light. Nat. Synth. 4, 673\u2013683 (2025). This article demonstrates how assembly state can be regulated intracellularly by the usage of a photocage in the visible light regime.","journal-title":"Nat. Synth."},{"key":"846_CR91","doi-asserted-by":"publisher","first-page":"3406","DOI":"10.1039\/C7CS00827A","volume":"47","author":"P Makam","year":"2018","unstructured":"Makam, P. & Gazit, E. Minimalistic peptide supramolecular co-assembly: expanding the conformational space for nanotechnology. Chem. Soc. Rev. 47, 3406\u20133420 (2018).","journal-title":"Chem. Soc. Rev."},{"key":"846_CR92","doi-asserted-by":"publisher","first-page":"1003","DOI":"10.1021\/acs.langmuir.9b02941","volume":"36","author":"VK Pal","year":"2020","unstructured":"Pal, V. K., Jain, R. & Roy, S. Tuning the supramolecular structure and function of collagen mimetic ionic complementary peptides via electrostatic interactions. Langmuir 36, 1003\u20131013 (2020).","journal-title":"Langmuir"},{"key":"846_CR93","doi-asserted-by":"publisher","first-page":"580","DOI":"10.1016\/j.jcis.2020.12.066","volume":"588","author":"M Criado-Gonzalez","year":"2021","unstructured":"Criado-Gonzalez, M. et al. Supramolecular tripeptide self-assembly initiated at the surface of coacervates by polyelectrolyte exchange. J. Colloid Interface Sci. 588, 580\u2013588 (2021).","journal-title":"J. Colloid Interface Sci."},{"key":"846_CR94","doi-asserted-by":"publisher","DOI":"10.1093\/rb\/rbab040","volume":"8","author":"A Ajovalasit","year":"2021","unstructured":"Ajovalasit, A. et al. Carboxylated-xyloglucan and peptide amphiphile co-assembly in wound healing. Regen. Biomater. 8, rbab040 (2021).","journal-title":"Regen. Biomater."},{"key":"846_CR95","doi-asserted-by":"publisher","first-page":"1812","DOI":"10.1126\/science.1154586","volume":"319","author":"RM Capito","year":"2008","unstructured":"Capito, R. M., Azevedo, H. S., Velichko, Y. S., Mata, A. & Stupp, S. I. Self-assembly of large and small molecules into hierarchically ordered sacs and membranes. Science 319, 1812\u20131816 (2008).","journal-title":"Science"},{"key":"846_CR96","doi-asserted-by":"publisher","DOI":"10.1016\/j.mtbio.2023.100598","volume":"19","author":"Y Yuan","year":"2023","unstructured":"Yuan, Y., Shi, Y., Banerjee, J., Sadeghpour, A. & Azevedo, H. S. Structuring supramolecular hyaluronan hydrogels via peptide self-assembly for modulating the cell microenvironment. Mater. Today Bio 19, 100598 (2023).","journal-title":"Mater. Today Bio"},{"key":"846_CR97","doi-asserted-by":"publisher","first-page":"8753","DOI":"10.1039\/C4RA16593D","volume":"5","author":"J Boekhoven","year":"2015","unstructured":"Boekhoven, J. et al. Alginate\u2013peptide amphiphile core\u2013shell microparticles as a targeted drug delivery system. RSC Adv. 5, 8753\u20138756 (2015).","journal-title":"RSC Adv."},{"key":"846_CR98","doi-asserted-by":"publisher","first-page":"4949","DOI":"10.1039\/D1SM00168J","volume":"17","author":"TJ Cotey","year":"2021","unstructured":"Cotey, T. J., Sai, H., Perez, C., Palmer, L. C. & Stupp, S. I. Hybrid gels via bulk interfacial complexation of supramolecular polymers and polyelectrolytes. Soft Matter 17, 4949\u20134956 (2021).","journal-title":"Soft Matter"},{"key":"846_CR99","doi-asserted-by":"publisher","first-page":"4646","DOI":"10.1021\/acsbiomaterials.9b00941","volume":"5","author":"E Radvar","year":"2019","unstructured":"Radvar, E. & Azevedo, H. S. Supramolecular nanofibrous peptide\/polymer hydrogels for the multiplexing of bioactive signals. ACS Biomater. Sci. Eng. 5, 4646\u20134656 (2019).","journal-title":"ACS Biomater. Sci. Eng."},{"key":"846_CR100","doi-asserted-by":"publisher","first-page":"897","DOI":"10.1038\/nchem.2349","volume":"7","author":"KE Inostroza-Brito","year":"2015","unstructured":"Inostroza-Brito, K. E. et al. Co-assembly, spatiotemporal control and morphogenesis of a hybrid protein\u2013peptide system. Nat. Chem. 7, 897\u2013904 (2015).","journal-title":"Nat. Chem."},{"key":"846_CR101","doi-asserted-by":"publisher","first-page":"4180","DOI":"10.1021\/acs.biomac.0c00984","volume":"21","author":"R Jain","year":"2020","unstructured":"Jain, R., Pal, V. K. & Roy, S. Triggering supramolecular hydrogelation using a protein\u2013peptide coassembly approach. Biomacromolecules 21, 4180\u20134193 (2020).","journal-title":"Biomacromolecules"},{"key":"846_CR102","doi-asserted-by":"publisher","first-page":"11657","DOI":"10.1021\/acs.langmuir.1c01376","volume":"37","author":"Y Ge","year":"2021","unstructured":"Ge, Y. et al. Coassembly behavior and rheological properties of a \u03b2-hairpin peptide with dicarboxylates. Langmuir 37, 11657\u201311664 (2021).","journal-title":"Langmuir"},{"key":"846_CR103","doi-asserted-by":"publisher","DOI":"10.1016\/j.colsurfb.2021.111673","volume":"202","author":"Z Gong","year":"2021","unstructured":"Gong, Z. et al. Tumor acidic microenvironment-induced drug release of RGD peptide nanoparticles for cellular uptake and cancer therapy. Colloids Surf. B Biointerfaces 202, 111673 (2021).","journal-title":"Colloids Surf. B Biointerfaces"},{"key":"846_CR104","doi-asserted-by":"publisher","first-page":"7034","DOI":"10.1021\/acs.chemmater.8b02572","volume":"30","author":"W He","year":"2018","unstructured":"He, W. et al. Peptide-induced self-assembly of therapeutics into a well-defined nanoshell with tumor-triggered shape and charge switch. Chem. Mater. 30, 7034\u20137046 (2018).","journal-title":"Chem. Mater."},{"key":"846_CR105","doi-asserted-by":"publisher","first-page":"3513","DOI":"10.1021\/acs.langmuir.8b03175","volume":"35","author":"L Zhang","year":"2019","unstructured":"Zhang, L. et al. Histidine-rich cell-penetrating peptide for cancer drug delivery and its uptake mechanism. Langmuir 35, 3513\u20133523 (2019).","journal-title":"Langmuir"},{"key":"846_CR106","doi-asserted-by":"publisher","first-page":"11686","DOI":"10.1021\/acsnano.9b05608","volume":"13","author":"J Wang","year":"2019","unstructured":"Wang, J. et al. pH-switchable antimicrobial nanofiber networks of hydrogel eradicate biofilm and rescue stalled healing in chronic wounds. ACS Nano 13, 11686\u201311697 (2019).","journal-title":"ACS Nano"},{"key":"846_CR107","doi-asserted-by":"publisher","first-page":"3648","DOI":"10.1021\/acsabm.0c00281","volume":"3","author":"X Sha","year":"2020","unstructured":"Sha, X. et al. Self-assembled peptide nanofibrils designed to release membrane-lysing antimicrobial peptides. ACS Appl. Bio Mater. 3, 3648\u20133655 (2020).","journal-title":"ACS Appl. Bio Mater."},{"key":"846_CR108","doi-asserted-by":"publisher","first-page":"6415","DOI":"10.1021\/acsabm.5c00897","volume":"8","author":"H Asokan-Sheeja","year":"2025","unstructured":"Asokan-Sheeja, H. et al. pH-responsive peptide\u2013polymer hydrogel for biofilm disruption. ACS Appl. Bio Mater. 8, 6415\u20136425 (2025).","journal-title":"ACS Appl. Bio Mater."},{"key":"846_CR109","doi-asserted-by":"publisher","first-page":"6800","DOI":"10.1021\/acsbiomaterials.0c01485","volume":"6","author":"T Wang","year":"2020","unstructured":"Wang, T. et al. Smart adhesive peptide nanofibers for cell capture and release. ACS Biomater. Sci. Eng. 6, 6800\u20136807 (2020).","journal-title":"ACS Biomater. Sci. Eng."},{"key":"846_CR110","doi-asserted-by":"publisher","first-page":"1376","DOI":"10.1002\/cbic.201800781","volume":"20","author":"M Pieszka","year":"2019","unstructured":"Pieszka, M., Sobota, A. M., Ga\u010danin, J., Weil, T. & Ng, D. Y. W. Orthogonally stimulated assembly\/disassembly of depsipeptides by rational chemical design. ChemBioChem 20, 1376\u20131381 (2019).","journal-title":"ChemBioChem"},{"key":"846_CR111","doi-asserted-by":"publisher","DOI":"10.1002\/marc.201900476","volume":"41","author":"CM Berac","year":"2020","unstructured":"Berac, C. M. et al. Evaluation of charge-regulated supramolecular copolymerization to tune the time scale for oxidative disassembly of \u03b2-sheet comonomers. Macromol. Rapid Commun. 41, 1900476 (2020).","journal-title":"Macromol. Rapid Commun."},{"key":"846_CR112","doi-asserted-by":"publisher","DOI":"10.1002\/cbic.202200798","volume":"24","author":"Y Hara","year":"2023","unstructured":"Hara, Y., Yaguchi, A., Hiramatsu, H. & Muraoka, T. ROS-triggered gel\u2013sol transition and kinetics-controlled cargo release by methionine-containing peptides. ChemBioChem 24, e202200798 (2023).","journal-title":"ChemBioChem"},{"key":"846_CR113","doi-asserted-by":"publisher","first-page":"395","DOI":"10.1016\/j.jcis.2022.01.181","volume":"615","author":"M Cao","year":"2022","unstructured":"Cao, M. et al. Peptide self-assembly into stable capsid-like nanospheres and co-assembly with DNA to produce smart artificial viruses. J. Colloid Interface Sci. 615, 395\u2013407 (2022).","journal-title":"J. Colloid Interface Sci."},{"key":"846_CR114","doi-asserted-by":"publisher","first-page":"6517","DOI":"10.1039\/D2BM01120D","volume":"10","author":"L Zhang","year":"2022","unstructured":"Zhang, L. et al. Sequential self-assembly and disassembly of curcumin hydrogel effectively alleviates inflammatory bowel disease. Biomater. Sci. 10, 6517\u20136524 (2022).","journal-title":"Biomater. Sci."},{"key":"846_CR115","doi-asserted-by":"publisher","first-page":"3950","DOI":"10.1021\/jacs.7b00070","volume":"139","author":"Z Feng","year":"2017","unstructured":"Feng, Z., Wang, H., Zhou, R., Li, J. & Xu, B. Enzyme-instructed assembly and disassembly processes for targeting downregulation in cancer cells. J. Am. Chem. Soc. 139, 3950\u20133953 (2017).","journal-title":"J. Am. Chem. Soc."},{"key":"846_CR116","doi-asserted-by":"publisher","first-page":"1944","DOI":"10.1039\/C9TB02625H","volume":"8","author":"Y Dai","year":"2020","unstructured":"Dai, Y. et al. Co-assembly of curcumin and a cystine bridged peptide to construct tumor-responsive nano-micelles for efficient chemotherapy. J. Mater. Chem. B 8, 1944\u20131951 (2020).","journal-title":"J. Mater. Chem. B"},{"key":"846_CR117","doi-asserted-by":"publisher","first-page":"5374","DOI":"10.1021\/acs.biomac.1c01324","volume":"22","author":"L Dong","year":"2021","unstructured":"Dong, L. et al. Poly(L-cysteine) peptide amphiphile derivatives containing disulfide bonds: synthesis, self-assembly-induced \u03b2-sheet nanostructures, pH\/reduction dual response, and drug release. Biomacromolecules 22, 5374\u20135381 (2021).","journal-title":"Biomacromolecules"},{"key":"846_CR118","doi-asserted-by":"publisher","first-page":"459","DOI":"10.1021\/acsnano.5c13501","volume":"20","author":"S Ren","year":"2026","unstructured":"Ren, S. et al. Redox-responsive peptide coacervates for enhanced mRNA delivery and intracellular release. ACS Nano 20, 459\u2013474 (2026).","journal-title":"ACS Nano"},{"key":"846_CR119","doi-asserted-by":"publisher","first-page":"8860","DOI":"10.1002\/anie.201916111","volume":"59","author":"J Yang","year":"2020","unstructured":"Yang, J. et al. Hierarchical self-assembled photo-responsive tubisomes from a cyclic peptide-bridged amphiphilic block copolymer. Angew. Chem. Int. Ed. 59, 8860\u20138863 (2020).","journal-title":"Angew. Chem. Int. Ed."},{"key":"846_CR120","doi-asserted-by":"publisher","first-page":"822","DOI":"10.1038\/nm0798-822","volume":"4","author":"C Soto","year":"1998","unstructured":"Soto, C. et al. \u03b2-Sheet breaker peptides inhibit fibrillogenesis in a rat brain model of amyloidosis: implications for Alzheimer\u2019s therapy. Nat. Med. 4, 822\u2013826 (1998).","journal-title":"Nat. Med."},{"key":"846_CR121","doi-asserted-by":"publisher","first-page":"119","DOI":"10.3109\/13506129.2011.582902","volume":"18","author":"A Frydman-Marom","year":"2011","unstructured":"Frydman-Marom, A., Shaltiel-Karyo, R., Moshe, S. & Gazit, E. The generic amyloid formation inhibition effect of a designed small aromatic \u03b2-breaking peptide. Amyloid 18, 119\u2013127 (2011).","journal-title":"Amyloid"},{"key":"846_CR122","doi-asserted-by":"publisher","first-page":"2993","DOI":"10.1039\/D3NR04847K","volume":"16","author":"S Dinda","year":"2024","unstructured":"Dinda, S., Ghosh, D. & Govindaraju, T. Cooperative dissolution of peptidomimetic vesicles and amyloid \u03b2 fibrils. Nanoscale. 16, 2993\u20133005 (2024).","journal-title":"Nanoscale."},{"key":"846_CR123","doi-asserted-by":"publisher","first-page":"14415","DOI":"10.1021\/ja052806a","volume":"127","author":"M Fokkens","year":"2005","unstructured":"Fokkens, M., Schrader, T. & Kl\u00e4rner, F. G. A molecular tweezer for lysine and arginine. J. Am. Chem. Soc. 127, 14415\u201314421 (2005).","journal-title":"J. Am. Chem. Soc."},{"key":"846_CR124","doi-asserted-by":"publisher","first-page":"16958","DOI":"10.1021\/ja206279b","volume":"133","author":"S Sinha","year":"2011","unstructured":"Sinha, S. et al. Lysine-specific molecular tweezers are broad-spectrum inhibitors of assembly and toxicity of amyloid proteins. J. Am. Chem. Soc. 133, 16958\u201316969 (2011).","journal-title":"J. Am. Chem. Soc."},{"key":"846_CR125","doi-asserted-by":"publisher","first-page":"4831","DOI":"10.1021\/acs.jpcb.5b00692","volume":"119","author":"X Zheng","year":"2015","unstructured":"Zheng, X. et al. Amyloid \u03b2-protein assembly: the effect of molecular tweezers CLR01 and CLR03. J. Phys. Chem. B 119, 4831\u20134841 (2015).","journal-title":"J. Phys. Chem. B"},{"key":"846_CR126","doi-asserted-by":"publisher","first-page":"11939","DOI":"10.1039\/D4TB01575D","volume":"12","author":"C Ligorio","year":"2024","unstructured":"Ligorio, C. et al. Disassembly of self-assembling peptide hydrogels as a versatile method for cell extraction and manipulation. J. Mater. Chem. B 12, 11939\u201311952 (2024).","journal-title":"J. Mater. Chem. B"},{"key":"846_CR127","doi-asserted-by":"publisher","DOI":"10.1038\/s41467-023-40663-6","volume":"14","author":"K Kaygisiz","year":"2023","unstructured":"Kaygisiz, K. et al. Data-mining unveils structure\u2013property\u2013activity correlation of viral infectivity enhancing self-assembling peptides. Nat. Commun. 14, 5121 (2023).","journal-title":"Nat. Commun."},{"key":"846_CR128","doi-asserted-by":"publisher","first-page":"5251","DOI":"10.1039\/D3BM00412K","volume":"11","author":"K Kaygisiz","year":"2023","unstructured":"Kaygisiz, K. et al. Inverse design of viral infectivity-enhancing peptide fibrils from continuous protein-vector embeddings. Biomater. Sci. 11, 5251\u20135261 (2023).","journal-title":"Biomater. Sci."},{"key":"846_CR129","doi-asserted-by":"publisher","first-page":"20295","DOI":"10.1021\/acsnano.5c00670","volume":"19","author":"E Dra\u017ei\u0107","year":"2025","unstructured":"Dra\u017ei\u0107, E., Jelu\u0161i\u0107, D., Jankovi\u0107 Bevandi\u0107, P., Mau\u0161a, G. & Kalafatovic, D. Using machine learning to fast-track peptide nanomaterial discovery. ACS Nano 19, 20295\u201320320 (2025).","journal-title":"ACS Nano"},{"key":"846_CR130","doi-asserted-by":"publisher","first-page":"266","DOI":"10.1126\/science.adf6591","volume":"380","author":"ID Lutz","year":"2023","unstructured":"Lutz, I. D. et al. Top\u2013down design of protein architectures with reinforcement learning. Science 380, 266\u2013273 (2023).","journal-title":"Science"},{"key":"846_CR131","doi-asserted-by":"publisher","DOI":"10.1038\/s41467-023-39648-2","volume":"14","author":"T Xu","year":"2023","unstructured":"Xu, T. et al. Accelerating the prediction and discovery of peptide hydrogels with human-in-the-loop. Nat. Commun. 14, 3880 (2023).","journal-title":"Nat. Commun."},{"key":"846_CR132","doi-asserted-by":"publisher","first-page":"1295","DOI":"10.1038\/s41563-025-02164-3","volume":"24","author":"H Liu","year":"2025","unstructured":"Liu, H. et al. De novo design of self-assembling peptides with antimicrobial activity guided by deep learning. Nat. Mater. 24, 1295\u20131306 (2025).","journal-title":"Nat. Mater."},{"key":"846_CR133","doi-asserted-by":"publisher","first-page":"2418","DOI":"10.1126\/science.1070821","volume":"295","author":"GM Whitesides","year":"2002","unstructured":"Whitesides, G. M. & Grzybowski, B. Self-assembly at all scales. Science 295, 2418\u20132421 (2002).","journal-title":"Science"},{"key":"846_CR134","doi-asserted-by":"publisher","first-page":"552","DOI":"10.1016\/j.chempr.2019.11.008","volume":"6","author":"B Rie\u00df","year":"2020","unstructured":"Rie\u00df, B., Gr\u00f6tsch, R. K. & Boekhoven, J. The design of dissipative molecular assemblies driven by chemical reaction cycles. Chem 6, 552\u2013578 (2020).","journal-title":"Chem"},{"key":"846_CR135","doi-asserted-by":"publisher","DOI":"10.1002\/anie.202400495","volume":"63","author":"S Borsley","year":"2024","unstructured":"Borsley, S., Leigh, D. A. & Roberts, B. M. W. Molecular ratchets and kinetic asymmetry: giving chemistry direction. Angew. Chem. Int. Ed. 63, e202400495 (2024).","journal-title":"Angew. Chem. Int. Ed."},{"key":"846_CR136","doi-asserted-by":"publisher","first-page":"5570","DOI":"10.1039\/C7CS00030H","volume":"46","author":"H Hess","year":"2017","unstructured":"Hess, H. & Ross, J. L. Non-equilibrium assembly of microtubules: from molecules to autonomous chemical robots. Chem. Soc. Rev. 46, 5570\u20135587 (2017).","journal-title":"Chem. Soc. Rev."},{"key":"846_CR137","doi-asserted-by":"publisher","first-page":"12653","DOI":"10.1039\/D3SC04281B","volume":"14","author":"X Chen","year":"2023","unstructured":"Chen, X., Soria-Carrera, H., Zozulia, O. & Boekhoven, J. Suppressing catalyst poisoning in the carbodiimide-fueled reaction cycle. Chem. Sci. 14, 12653\u201312660 (2023).","journal-title":"Chem. Sci."},{"key":"846_CR138","doi-asserted-by":"publisher","first-page":"6880","DOI":"10.1021\/jacs.3c00273","volume":"145","author":"X Chen","year":"2023","unstructured":"Chen, X. et al. A carbodiimide-fueled reaction cycle that forms transient 5(4H)-oxazolones. J. Am. Chem. Soc. 145, 6880\u20136887 (2023).","journal-title":"J. Am. Chem. Soc."},{"key":"846_CR139","doi-asserted-by":"publisher","first-page":"4121","DOI":"10.1039\/D0CS01148G","volume":"51","author":"HE Morgan","year":"2022","unstructured":"Morgan, H. E., Turnbull, W. B. & Webb, M. E. Challenges in the use of sortase and other peptide ligases for site-specific protein modification. Chem. Soc. Rev. 51, 4121\u20134145 (2022).","journal-title":"Chem. Soc. Rev."},{"key":"846_CR140","doi-asserted-by":"publisher","first-page":"16789","DOI":"10.1021\/ja4086353","volume":"135","author":"S Debnath","year":"2013","unstructured":"Debnath, S., Roy, S. & Ulijn, R. V. Peptide nanofibers with dynamic instability through nonequilibrium biocatalytic assembly. J. Am. Chem. Soc. 135, 16789\u201316792 (2013).","journal-title":"J. Am. Chem. Soc."},{"key":"846_CR141","doi-asserted-by":"publisher","first-page":"2213","DOI":"10.1021\/nl5039506","volume":"15","author":"T Heuser","year":"2015","unstructured":"Heuser, T., Steppert, A. K., Molano Lopez, C., Zhu, B. & Walther, A. Generic concept to program the time domain of self-assemblies with a self-regulation mechanism. Nano Lett. 15, 2213\u20132219 (2015).","journal-title":"Nano Lett."},{"key":"846_CR142","doi-asserted-by":"publisher","first-page":"13258","DOI":"10.1002\/anie.201505013","volume":"54","author":"T Heuser","year":"2015","unstructured":"Heuser, T. et al. Biocatalytic feedback-driven temporal programming of self-regulating peptide hydrogels. Angew. Chem. Int. Ed. 54, 13258\u201313262 (2015).","journal-title":"Angew. Chem. Int. Ed."},{"key":"846_CR143","doi-asserted-by":"publisher","first-page":"1125","DOI":"10.1039\/D2CC06402B","volume":"59","author":"C Sharma","year":"2023","unstructured":"Sharma, C., Maity, I. & Walther, A. pH-feedback systems to program autonomous self-assembly and material lifecycles. Chem. Commun. 59, 1125\u20131144 (2023).","journal-title":"Chem. Commun."},{"key":"846_CR144","doi-asserted-by":"publisher","first-page":"14194","DOI":"10.1039\/C9CC07358B","volume":"55","author":"B Saha","year":"2019","unstructured":"Saha, B., Chatterjee, A., Reja, A. & Das, D. Condensates of short peptides and ATP for the temporal regulation of cytochrome c activity. Chem. Commun. 55, 14194\u201314197 (2019).","journal-title":"Chem. Commun."},{"key":"846_CR145","doi-asserted-by":"publisher","DOI":"10.1002\/anie.202412534","volume":"63","author":"A-L Holtmannsp\u00f6tter","year":"2024","unstructured":"Holtmannsp\u00f6tter, A.-L. et al. Regulating nucleic acid catalysis using active droplets. Angew. Chem. Int. Ed. 63, e202412534 (2024). This article demonstrates how active droplets can be used to steer activity of catalytically active DNA.","journal-title":"Angew. Chem. Int. Ed."},{"key":"846_CR146","doi-asserted-by":"publisher","first-page":"330","DOI":"10.1021\/jacs.3c09202","volume":"146","author":"H Wang","year":"2023","unstructured":"Wang, H. et al. Organelle-mediated dissipative self-assembly of peptides in living cells. J. Am. Chem. Soc. 146, 330\u2013341 (2023).","journal-title":"J. Am. Chem. Soc."},{"key":"846_CR147","doi-asserted-by":"publisher","first-page":"4893","DOI":"10.1039\/D2SC01069K","volume":"13","author":"J Wang","year":"2022","unstructured":"Wang, J. et al. A reversible plasmonic nanoprobe for dynamic imaging of intracellular pH during endocytosis. Chem. Sci. 13, 4893\u20134901 (2022).","journal-title":"Chem. Sci."},{"key":"846_CR148","doi-asserted-by":"publisher","DOI":"10.1002\/anie.202409169","volume":"63","author":"P Zhao","year":"2024","unstructured":"Zhao, P. et al. Non-equilibrium dissipative assembly with switchable biological functions. Angew. Chem. Int. Ed. 63, e202409169 (2024).","journal-title":"Angew. Chem. Int. Ed."}],"container-title":["Nature Reviews Chemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.nature.com\/articles\/s41570-026-00846-3.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/www.nature.com\/articles\/s41570-026-00846-3","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/www.nature.com\/articles\/s41570-026-00846-3.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,8,6]],"date-time":"2026-08-06T12:01:22Z","timestamp":1786017682000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.nature.com\/articles\/s41570-026-00846-3"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,7,15]]},"references-count":148,"journal-issue":{"issue":"8","published-online":{"date-parts":[[2026,8]]}},"alternative-id":["846"],"URL":"https:\/\/doi.org\/10.1038\/s41570-026-00846-3","relation":{},"ISSN":["2397-3358"],"issn-type":[{"value":"2397-3358","type":"electronic"}],"subject":[],"published":{"date-parts":[[2026,7,15]]},"assertion":[{"value":"8 June 2026","order":1,"name":"accepted","label":"Accepted","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"15 July 2026","order":2,"name":"first_online","label":"First Online","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"The authors declare no competing interests.","order":1,"name":"Ethics","label":"Competing interests","group":{"name":"EthicsHeading","label":"Ethics"}}]}}