Amphipathic design dictates self-assembly, cytotoxicity and cell uptake of arginine-rich surfactant-like peptides

Simple item page
dc.contributorAalto-yliopistofi
dc.contributorAalto Universityen
dc.contributor.authorMello, Lucas R.
dc.contributor.authorAguiar, Rodrigo B.
dc.contributor.authorYamada, Renata Y.
dc.contributor.authorMoraes, Jane Z.
dc.contributor.authorHamley, Ian W.
dc.contributor.authorAlves, Wendel A.
dc.contributor.authorReza, Mehedi
dc.contributor.authorRuokolainen, Janne
dc.contributor.authorSilva, Emerson R.
dc.contributor.departmentUniversidade Federal de São Paulo
dc.contributor.departmentUniversity of Reading
dc.contributor.departmentUniversidade Federal do ABC
dc.contributor.departmentDepartment of Applied Physics
dc.contributor.departmentMolecular Materials
dc.date.accessioned2020-11-30T08:18:30Z
dc.date.available2020-11-30T08:18:30Z
dc.date.embargoinfo:eu-repo/date/embargoEnd/2021-02-22
dc.date.issued2020-03-28
dc.description.abstractAmphiphilicity is the most critical parameter in the self-assembly of surfactant-like peptides (SLPs), regulating the way by which hydrophobic attraction holds peptides together. Its effects go beyond supramolecular assembly and may also trigger different cell responses of bioactive peptide-based nanostructures. Herein, we investigate the self-assembly and cellular effects of nanostructures based on isomeric SLPs composed by arginine (R) and phenylalanine (F). Two amphipathic designs were studied: a diblock construct F4R4 and its bolaamphiphile analog R2F4R2. A strong sequence-dependent polymorphism emerges with appearance of globules and vesicle-like assemblies, or flat nanotapes and cylindrical micelles. The diblock construct possesses good cell penetrating capabilities and effectiveness to kill SK-MEL-28 melanoma tumor cells, in contrast to reduced intracellular uptake and low cytotoxicity exhibited by the bolaamphiphilic form. Our findings demonstrate that amphipathic design is a relevant variable for self-assembling SLPs to modulate different cellular responses and may assist in optimizing the production of nanostructures based on arginine-enriched sequences in cell penetrating and antimicrobial peptides.en
dc.description.versionPeer revieweden
dc.format.extent13
dc.format.extent2495-2507
dc.identifier.citationMello , L R , Aguiar , R B , Yamada , R Y , Moraes , J Z , Hamley , I W , Alves , W A , Reza , M , Ruokolainen , J & Silva , E R 2020 , ' Amphipathic design dictates self-assembly, cytotoxicity and cell uptake of arginine-rich surfactant-like peptides ' , Journal of Materials Chemistry B , vol. 8 , no. 12 , pp. 2495-2507 . https://doi.org/10.1039/c9tb02219hen
dc.identifier.doi10.1039/c9tb02219h
dc.identifier.issn2050-750X
dc.identifier.otherPURE UUID: b663cdfd-36b5-4e32-8e4a-ff38e2568c63
dc.identifier.otherPURE ITEMURL: https://research.aalto.fi/en/publications/b663cdfd-36b5-4e32-8e4a-ff38e2568c63
dc.identifier.otherPURE LINK: http://www.scopus.com/inward/record.url?scp=85082400971&partnerID=8YFLogxK
dc.identifier.otherPURE LINK: http://centaur.reading.ac.uk/90472/
dc.identifier.urihttps://aaltodoc.aalto.fi/handle/123456789/61784
dc.identifier.urnURN:NBN:fi:aalto-2020113020629
dc.language.isoenen
dc.publisherRoyal Society of Chemistry
dc.relation.ispartofseriesJournal of Materials Chemistry Ben
dc.relation.ispartofseriesVolume 8, issue 12en
dc.rightsopenAccessen
dc.titleAmphipathic design dictates self-assembly, cytotoxicity and cell uptake of arginine-rich surfactant-like peptidesen
dc.typeA1 Alkuperäisartikkeli tieteellisessä aikakauslehdessäfi
Files
Collections
[article-cris] Perustieteiden korkeakoulu / SCI