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dc.contributor.authorLim, Jessicaen_US
dc.contributor.authorKumar, Akshitaen_US
dc.contributor.authorLow, Kimberly Jia Yien_US
dc.contributor.authorVerma, Chandra Shekharen_US
dc.contributor.authorMu, Yuguangen_US
dc.contributor.authorMiserez, Alien_US
dc.contributor.authorPervushin, Konstantinen_US
dc.identifier.citationLim, J., Kumar, A., Low, K. J. Y., Verma, C. S., Mu, Y., Miserez, A. & Pervushin, K. (2021). Liquid-liquid phase separation of short histidine- and tyrosine-rich peptides: sequence specificity and molecular topology. Journal of Physical Chemistry B, 125(25), 6776-6790.
dc.description.abstractThe increasing realization of the prevalence of liquid-liquid phase separation (LLPS) across multiple length scales of biological constructs, from intracellular membraneless organelles to extracellular load-bearing tissues, has raised intriguing questions about intermolecular interactions regulating LLPS at the atomic level. Squid-beak derived histidine (His)- and tyrosine (Tyr)-rich peptides (HBpeps) have recently emerged as suitable short model peptides to precisely assess the roles of peptide motifs and single residues on the phase behavior and material properties of microdroplets obtained by LLPS. In this study, by systematically introducing single mutations in an HBpep, we have identified specific sticker residues that attract peptide chains together. We find that His and Tyr residues located near the sequence termini drive phase separation, forming interaction nodes that stabilize microdroplets. Combining quantum chemistry simulations with NMR studies, we predict atomic-level bond geometries and uncover inter-residue supramolecular interactions governing LLPS. These results are subsequently used to propose possible topological arrangements of the peptide chains, which upon expansion can help explain the three-dimensional network of microdroplets. The stability of the proposed topologies carried out through all-atom molecular dynamics simulations predicts chain topologies that are more likely to stabilize the microdroplets. Overall, this study provides useful guidelines for the de novo design of peptide coacervates with tunable phase behavior and material properties. In addition, the analysis of nanoscale topologies may pave the way to understand how client molecules can be trapped within microdroplets, with direct implications for the encapsulation and controlled release of therapeutics for drug delivery applications.en_US
dc.description.sponsorshipMinistry of Education (MOE)en_US
dc.relationMOE 2019-T3-1-012en_US
dc.relation.ispartofJournal of Physical Chemistry Ben_US
dc.rights© 2021 American Chemical Society. All rights reserved.en_US
dc.subjectEngineering::Chemical engineeringen_US
dc.titleLiquid-liquid phase separation of short histidine- and tyrosine-rich peptides: sequence specificity and molecular topologyen_US
dc.typeJournal Articleen
dc.contributor.schoolSchool of Biological Sciencesen_US
dc.contributor.schoolSchool of Materials Science and Engineeringen_US
dc.contributor.organizationBioinformatics Institute, A*STARen_US
dc.contributor.organizationNational University of Singaporeen_US
dc.contributor.researchBiological & Biomimetic Material Laboratory @ NTUen_US
dc.contributor.researchCenter for Sustainable Materialsen_US
dc.subject.keywordsAromatic Residuesen_US
dc.description.acknowledgementThis research was funded by the Singapore Ministry of Education (MOE) through an Academic Research Fund (AcRF) Tier 3 grant (grant no. MOE 2019-T3-1-012).en_US
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