{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,22]],"date-time":"2026-09-22T16:10:37Z","timestamp":1790093437064,"version":"4.0.1"},"reference-count":50,"publisher":"American Chemical Society (ACS)","issue":"37","license":[{"start":{"date-parts":[[2026,9,3]],"date-time":"2026-09-03T00:00:00Z","timestamp":1788393600000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by-nc-nd\/4.0\/"}],"funder":[{"DOI":"10.13039\/100012547","name":"Natural Science Foundation of Guangxi Zhuang Autonomous Region","doi-asserted-by":"publisher","award":["2026GXNSFHA00640263"],"award-info":[{"award-number":["2026GXNSFHA00640263"]}],"id":[{"id":"10.13039\/100012547","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100003819","name":"Natural Science Foundation of Hubei Province","doi-asserted-by":"publisher","award":["2026AFC0314"],"award-info":[{"award-number":["2026AFC0314"]}],"id":[{"id":"10.13039\/501100003819","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100012554","name":"Hubei Provincial Department of Education","doi-asserted-by":"publisher","award":["D20242104"],"award-info":[{"award-number":["D20242104"]}],"id":[{"id":"10.13039\/100012554","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001809","name":"National Natural Science Foundation of China","doi-asserted-by":"publisher","award":["11947006"],"award-info":[{"award-number":["11947006"]}],"id":[{"id":"10.13039\/501100001809","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2026,9,22]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>The liquid\u2013liquid phase separation (LLPS) of intrinsically disordered proteins is governed by a delicate balance among electrostatic, hydrophobic, and aromatic interactions, yet how residue identity reshapes this balance remains incompletely understood. Although significant progress has been made toward establishing a molecular grammar linking sequence to phase behavior, the specific roles of individual hydrophobic residues in modulating the electrostatic\u2013hydrophobic competition have not been systematically dissected. Here, we use a residue-level coarse-grained model to examine the phase behavior of artificially designed peptides with controlled charge patterning and amino acid composition. We find that even when the arrangement of charged and neutral residues is kept fixed, the identity of the neutral residue leads to qualitatively distinct phase behaviors. Phenylalanine monotonically enhances dense-phase formation, whereas alanine progressively suppresses it. In contrast, isoleucine produces a striking re-entrant behavior: increasing its fraction first weakens condensate formation by disrupting electrostatically stabilized associations, but beyond an intermediate composition, effective hydrophobic interactions become dominant and drive the re-emergence of a dense yet relatively loose and dynamic phase. These results illustrate that hydrophobic residues do not merely modulate LLPS strength, but can fundamentally alter the competition between interaction modes and thereby change the phase-separation regime. Our findings are consistent with a picture in which sequence composition modulates condensate formation via a balance among electrostatic, hydrophobic, and aromatic-type interactions, as captured by our coarse-grained model. Preliminary tests on LAF-1-RGG mutants further suggest that these trends may be transferable to biologically relevant IDRs. Together, this work provides additional insights into sequence-dependent LLPS and may inform the rational design of condensates with tunable material properties.<\/jats:p>","DOI":"10.1021\/acsomega.6c05668","type":"journal-article","created":{"date-parts":[[2026,9,3]],"date-time":"2026-09-03T21:02:30Z","timestamp":1788469350000},"page":"55921-55929","source":"Crossref","is-referenced-by-count":0,"title":["Electrostatic\u2013Hydrophobic\nCompetition Induces\nRe-Entrant Phase Separation in Designer Polypeptides"],"prefix":"10.1021","volume":"11","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-5465-6203","authenticated-orcid":true,"given":"Wen-Bin","family":"Kang","sequence":"first","affiliation":[{"name":"Hubei University of Medicine , , ,","place":["Shiyan, China, 442000"]},{"name":"Shiyan Key Laboratory of Intelligent Medicine Institute , ,","place":["Shiyan, China, 442000"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jia","family":"Guo","sequence":"additional","affiliation":[{"name":"Hubei University of Medicine , , ,","place":["Shiyan, China, 442000"]},{"name":"Shiyan Key Laboratory of Intelligent Medicine Institute , ,","place":["Shiyan, China, 442000"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Dan-Chen","family":"Wang","sequence":"additional","affiliation":[{"name":"Hubei University of Medicine , , ,","place":["Shiyan, China, 442000"]},{"name":"Shiyan Key Laboratory of Intelligent Medicine Institute , ,","place":["Shiyan, China, 442000"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-2804-8060","authenticated-orcid":true,"given":"Lei","family":"Bao","sequence":"additional","affiliation":[{"name":"Hubei University of Medicine , , ,","place":["Shiyan, China, 442000"]},{"name":"Shiyan Key Laboratory of Intelligent Medicine Institute , ,","place":["Shiyan, China, 442000"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ming-Chao","family":"Liu","sequence":"additional","affiliation":[{"name":"Hubei University of Medicine , , ,","place":["Shiyan, China, 442000"]},{"name":"Shiyan Key Laboratory of Intelligent Medicine Institute , ,","place":["Shiyan, China, 442000"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Lian-Tao","family":"Cheng","sequence":"additional","affiliation":[{"name":"Hubei University of Medicine , , ,","place":["Shiyan, China, 442000"]},{"name":"Shiyan Key Laboratory of Intelligent Medicine Institute , ,","place":["Shiyan, China, 442000"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Er-Bin","family":"He","sequence":"additional","affiliation":[{"name":"Yulin Normal University , , ,","place":["Yulin, China, 537000"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Gen","family":"Zhu","sequence":"additional","affiliation":[{"name":"Hubei University of Medicine , , ,","place":["Shiyan, China, 442000"]},{"name":"Shiyan Key Laboratory of Intelligent Medicine Institute , ,","place":["Shiyan, China, 442000"]}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"316","published-online":{"date-parts":[[2026,9,3]]},"reference":[{"issue":"6357","key":"2026092210563751200_cit1","doi-asserted-by":"publisher","DOI":"10.1126\/science.aaf4382","article-title":"Liquid phase condensation in cell physiology and disease","volume":"357","author":"Shin","year":"2017","journal-title":"Science"},{"issue":"3","key":"2026092210563751200_cit2","doi-asserted-by":"publisher","first-page":"419","DOI":"10.1016\/j.cell.2018.12.035","article-title":"Considerations and Challenges in\nStudying Liquid-Liquid Phase Separation and Biomolecular Condensates","volume":"176","author":"Alberti","year":"2019","journal-title":"Cell"},{"issue":"5","key":"2026092210563751200_cit3","doi-asserted-by":"publisher","first-page":"285","DOI":"10.1038\/nrm.2017.7","article-title":"Biomolecular\ncondensates:\norganizers of cellular biochemistry","volume":"18","author":"Banani","year":"2017","journal-title":"Nat. Rev.\nMol. Cell Biol."},{"issue":"6512","key":"2026092210563751200_cit4","doi-asserted-by":"publisher","first-page":"56","DOI":"10.1126\/science.abb8032","article-title":"Beyond aggregation: Pathological\nphase transitions in neurodegenerative disease","volume":"370","author":"Mathieu","year":"2020","journal-title":"Science"},{"issue":"11","key":"2026092210563751200_cit5","doi-asserted-by":"publisher","first-page":"899","DOI":"10.1038\/nphys3532","article-title":"Polymer physics of intracellular\nphase transitions","volume":"11","author":"Brangwynne","year":"2015","journal-title":"Nat. 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Soc."},{"key":"2026092210563751200_cit27","doi-asserted-by":"publisher","first-page":"E1","DOI":"10.1016\/j.bpj.2021.03.003","article-title":"Faces, Facets, and Functions of Biomolecular\nCondensates Driven by Multivalent Proteins and Nucleic Acids","volume":"120","author":"Kahn","year":"2021","journal-title":"Biophys. J."},{"key":"2026092210563751200_cit28","doi-asserted-by":"publisher","first-page":"1857","DOI":"10.1021\/acsami.5c20923","article-title":"From Cellular\nOrganization to Synthetic Platforms: Liquid\u2013Liquid\nPhase Separation as a Framework for Functional Biomolecular Condensates","volume":"17","author":"Deng","year":"2026","journal-title":"ACS Appl. Mater. Interfaces"},{"key":"2026092210563751200_cit29","doi-asserted-by":"publisher","first-page":"107","DOI":"10.1146\/annurev-biophys-121219-081629","article-title":"Physical Principles Underlying the\nComplex Biology of Intracellular Phase Transitions","volume":"49","author":"Choi","year":"2020","journal-title":"Annu. Rev. Biophys."},{"key":"2026092210563751200_cit30","doi-asserted-by":"publisher","first-page":"7130","DOI":"10.1021\/acs.jpcb.3c03087","article-title":"Decoupling of Interactions\nbetween Model-Charged Peptides Reveals\nKey Factors Responsible for Liquid\u2013Liquid Phase Separation","volume":"127","author":"Saha","year":"2023","journal-title":"J. Phys. Chem. B"},{"key":"2026092210563751200_cit31","doi-asserted-by":"publisher","first-page":"10386","DOI":"10.1021\/jacs.2c02222","article-title":"Formation of versus Recruitment to\nRNA-Rich Condensates: Controlling Effects Exerted by Peptide Side\nChain Identity","volume":"144","author":"Niu","year":"2022","journal-title":"J. Am. Chem. Soc."},{"issue":"9","key":"2026092210563751200_cit32","doi-asserted-by":"publisher","DOI":"10.1016\/j.xcrp.2021.100579","article-title":"Prediction\nand Characterization\nof Liquid-Liquid Phase Separation of Minimalistic Peptides","volume":"2","author":"Tang","year":"2021","journal-title":"Cell Rep. Phys. Sci."},{"key":"2026092210563751200_cit33","doi-asserted-by":"publisher","first-page":"732","DOI":"10.1038\/s43588-021-00155-3","article-title":"Physics-Driven\nCoarse-Grained Model for Biomolecular Phase Separation with Near-Quantitative\nAccuracy","volume":"1","author":"Joseph","year":"2021","journal-title":"Nat. Comput. Sci."},{"issue":"1","key":"2026092210563751200_cit34","doi-asserted-by":"publisher","first-page":"557","DOI":"10.1146\/annurev-physchem-082423-032133","article-title":"Computational Modeling of Bi-omolecular\nPhase Separation:\nCurrent progress and open challenges","volume":"77","author":"Rizuan","year":"2026","journal-title":"Annu.\nRev. Phys. 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Theory Comput."},{"key":"2026092210563751200_cit37","doi-asserted-by":"publisher","first-page":"1371","DOI":"10.1002\/pro.4094","article-title":"Improved Coarse-Grained\nModel for Studying Sequence Dependent Phase Separation of Disordered\nProteins","volume":"30","author":"Regy","year":"2021","journal-title":"Protein Sci."},{"key":"2026092210563751200_cit38","doi-asserted-by":"publisher","DOI":"10.1016\/j.commatsci.2019.109363","article-title":"HOOMD-blue:\nA Python Package for\nHigh-Performance Molecular Dynamics and Hard Particle Monte Carlo\nSimulations","volume":"173","author":"Anderson","year":"2020","journal-title":"Comput. Mater. Sci."},{"key":"2026092210563751200_cit39","unstructured":"Howard, M. 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Sci.\nU.S.A."},{"key":"2026092210563751200_cit41","first-page":"51","article-title":"Numerical Techniques for Applications\nof Analytical Theories to Sequence-Dependent Phase Separations of\nIntrinsically Disordered Proteins","volume-title":"Methods\nin Molecular Biology","author":"Lin","year":"2023"},{"issue":"3","key":"2026092210563751200_cit42","doi-asserted-by":"publisher","DOI":"10.1371\/journal.pcbi.1008672","article-title":"Thermodynamic and sequential\ncharacteristics of phase separation\nand droplet formation for an intrinsically disordered region\/protein\nensemble","volume":"17","author":"Chu","year":"2021","journal-title":"PLoS Comput. Biol."},{"issue":"2","key":"2026092210563751200_cit43","doi-asserted-by":"publisher","first-page":"950","DOI":"10.1021\/acs.jcim.4c02034","article-title":"Charge Arrangement\nDetermines the Sensitivity of Aggregation Patterns between Peptide-Chains\nto the Surrounding Ionic Environment","volume":"65","author":"Bao","year":"2025","journal-title":"J. Chem.\nInf Model."},{"issue":"41","key":"2026092210563751200_cit44","doi-asserted-by":"publisher","first-page":"7944","DOI":"10.1039\/D3SM00633F","article-title":"Multi-scale\nmolecular simulation\nof random peptide phase separation and its extended-to-compact structure\ntransition driven by hydrophobic interactions","volume":"19","author":"Kang","year":"2023","journal-title":"Soft Matter."},{"issue":"7","key":"2026092210563751200_cit45","doi-asserted-by":"publisher","first-page":"1113","DOI":"10.1038\/s41557-024-01489-x","article-title":"Expanding the molecular language\nof protein liquid-liquid phase separation","volume":"16","author":"Rekhi","year":"2024","journal-title":"Nat.\nChem."},{"key":"2026092210563751200_cit46","doi-asserted-by":"crossref","first-page":"189","DOI":"10.1016\/B978-0-12-816348-1.00006-5","article-title":"Modeling\nprotein-protein interactions with intrinsically disordered proteins","volume-title":"Intrinsically Disordered Proteins","author":"Christoffer","year":"2019"},{"issue":"10","key":"2026092210563751200_cit47","doi-asserted-by":"publisher","DOI":"10.1063\/1.3557059","article-title":"Re-entrant phase behavior for systems with competition\nbetween phase separation and self-assembly","volume":"134","author":"Reinhardt","year":"2011","journal-title":"J. Chem. Phys."},{"issue":"42","key":"2026092210563751200_cit48","doi-asserted-by":"publisher","first-page":"8483","DOI":"10.1039\/C9SM00998A","article-title":"Re-entrant phase separation in nematically aligning\nactive polar particles","volume":"15","author":"Bhattacherjee","year":"2019","journal-title":"Soft Matter"},{"issue":"5","key":"2026092210563751200_cit49","doi-asserted-by":"publisher","DOI":"10.1063\/5.0275344","article-title":"Unraveling the impact\nof interaction types on phase separation of intrinsically disordered\nprotein chains","volume":"163","author":"Chen","year":"2025","journal-title":"J. Chem. Phys."},{"issue":"5-1","key":"2026092210563751200_cit50","doi-asserted-by":"publisher","DOI":"10.1103\/PhysRevE.111.054403","article-title":"Sequence-dependent\nbiomolecular phase separation driven by short-range interaction: From\nmaterial properties to coarsening dynamics","volume":"111","author":"Li","year":"2025","journal-title":"Phys. Rev. E"}],"container-title":["ACS Omega"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/pubs.acs.org\/doi\/pdf\/10.1021\/acsomega.6c05668","content-type":"application\/pdf","content-version":"vor","intended-application":"unspecified"},{"URL":"https:\/\/pubs.acs.org\/acsodf\/article-pdf\/11\/37\/55921\/68290132\/acsomega.6c05668.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/pubs.acs.org\/acsodf\/article-pdf\/11\/37\/55921\/68290132\/acsomega.6c05668.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,9,22]],"date-time":"2026-09-22T15:44:15Z","timestamp":1790091855000},"score":1,"resource":{"primary":{"URL":"https:\/\/pubs.acs.org\/acsodf\/article\/11\/37\/55921\/5413695\/Electrostatic-Hydrophobic-Competition-Induces-Re"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,9,3]]},"references-count":50,"journal-issue":{"issue":"37","published-online":{"date-parts":[[2026,9,3]]},"published-print":{"date-parts":[[2026,9,22]]}},"URL":"https:\/\/doi.org\/10.1021\/acsomega.6c05668","relation":{},"ISSN":["2470-1343"],"issn-type":[{"value":"2470-1343","type":"electronic"}],"subject":[],"published":{"date-parts":[[2026,9,3]]}}}