Pharmaceutical Research

, Volume 5, Issue 3, pp 140–150

The Role of Protein and Lipid Domains in the Uptake of Solutes by Human Stratum Corneum


  • Prakash V. Raykar
    • Department of Pharmaceutics, College of PharmacyUniversity of Utah
  • Man-Cheong Fung
    • Department of Pharmaceutics, College of PharmacyUniversity of Utah
  • Bradley D. Anderson
    • Department of Pharmaceutics, College of PharmacyUniversity of Utah

DOI: 10.1023/A:1015956705293

Cite this article as:
Raykar, P.V., Fung, M. & Anderson, B.D. Pharm Res (1988) 5: 140. doi:10.1023/A:1015956705293


The uptake of a series of hydrocortisone esters varying in lipophilicity from water into untreated and delipidized human stratum corneum has been determined. The partition coefficients of solutes into fully hydrated stratum corneum are postulated to represent the separate contributions of three structurally distinct domains—the extractable lipids, protein, and the solvent domain. The solvent domain was assumed to have the properties of bulk water. The relative affinities of the protein and lipid domains of stratum corneum for solutes varying in structure were determined by comparing solute uptake in untreated and delipidized stratum corneum. Partitioning into the extracted lipids was also examined. Solute uptake into stratum corneum may be governed by the protein domain, the lipid domain, or a combination of the two, depending on solute lipophilicity. Due to differences in the selectivity of the two domains, a change in uptake mechanism occurs with increasing solute lipophilicity from protein-dominated uptake for hydrophilic solutes to lipid domain-dominated uptake for lipophilic solutes. The stratum corneum lipid content, which varies dramatically from individual to individual (3–46% in this study), is an important determinant of the affinity of the stratum corneum for highly lipophilic solutes but has no effect on the uptake of hydrophilic solutes.

stratum corneumpartition coefficientshydrocortisone esterslipids, proteinuptakewater of hydration

Copyright information

© Plenum Publishing Corporation 1988