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1、RSCAdvancesViewArticleOnlinePAPERViewJournal
2、ViewIssueChangingtheshapeofhairwithkeratinpeptides†aaabaaCitethis:RSCAdv.,2017,7,51581C.F.Cruz,‡M.Martins,‡J.Egipto,H.Osorio,´A.RibeiroandA.Cavaco-Paulo*Chemicalstraighteningofcurlyhumanhairfibresinvolvestheuseofstrongreducingagentsatalka
3、linepH.Humanhairismadeofkeratin,andthefixationoffibreshapeinvolvesthereductionandreformationofnewdisulphidebondsbetweenkeratinmolecules.Here,weproposeanalternativeandgreenmethodologyusingkeratinpeptidesequences(10–13residues)derivedfromthehumangenome.Inapreviousstudy,weanalysed1235cy
4、steine-containingpeptidesencodedbyallhumangenesofhairkeratinandkeratin-associatedproteins.Thesepeptidefragmentshavebeendesignedbynaturetointeractwithkeratin.Herewetestedeightpeptides,whichwereselectbasedontheiraffinityforhumanhairkeratinsolutionasshownbyMatrix-AssistedLaser-Desorptio
5、nIonizationTime-of-FlightMassSpectrometry(MALDI-TOF/TOF)andbymoleculardynamicssimulation.Thepeptideswerecharacterizedindetailregardingtheirabilitytoactashairstraighteningmodulatorsandtoimprovethetensilestrengthandelasticityofhair.Oftheeighttestedpeptides,PepE,PepGandKPshowedthehigh
6、estabilitytointeractwithCreativeCommonsAttribution-NonCommercial3.0UnportedLicence.akeratinpeptidemodel,andtoimprovehairmechanicalpropertiesandstraighteningefficiency.TheproposedsolutionspresentedherewillreplaceharshreducingagentsatalkalinepHbypeptideReceived20thSeptember2017formulat
7、ionsactingatneutralpHtochangehairshapethroughthere-conformationofdisulphideAccepted26thOctober2017bonds.Here,weprovideexperimentalevidencewhichexplainsatamolecularlevelhowkeratinDOI:10.1039/c7ra10461hdecapeptidescaninteractwithlargekeratinmoleculesinhumanhair,openinganinnovativegre
8、enrsc.li/rsc-advancesapproachtochangingtheshapeofhairfibre.IntroductionrepeatedhairchemicaltreatmentsproduceirreversiblechangesThisarticleislicensedunderainhairtexture,andcanresultinafractureofthehairbreonceThehaircareindustryhasdevelopedaplethoraofproductstothecuticleisremoved,and
9、cortexexposureleadstobreak