International Journal of Cosmetic Science · 1984 · 68 citations · 20 references
Life SciencesBiochemistryDrug DeliveryProtein BiochemistryStructure-activity RelationshipsChromatographyProtein DenaturationSurfactantsAmphoteric SurfactantsAnionic SurfactantsAssay ReproducibilityChemical PropertiesHydrophobic InteractionsPhysicochemical PropertiesProtein Denaturation EffectsSurfactant Systems
Synopsis Protein denaturation was investigated to establish an in vitro evaluation method of surfactants in connection with their in vivo irritation potency to human skin. Eventually a new method with simplicity and high reproducibility was established by using quantitative analysis with gel-permeation chromatography (GPC). The protein denaturing potency of the commercially available surfactants was measured by using the developed method. Synergistic reduction in protein denaturation was observed in the mixed systems of anionic and amphoteric surfactants. The synergistic reduction was explained in terms of the physico-chemical properties of the mixed surfactants. A possible mechanism is the remarkable lowering of the total monomer concentration by the formation of hydrophobic complexes between the anionic and amphoteric surfactants.
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THE MECHANISM OF WATER BINDING IN STRATUM CORNEUM
John Middleton · British Journal of Dermatology · 1968 · 135 citations
Engineering, Dermatology, Physiology +16