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Protein conformational changes induced in human stratum corneum by organic sulfoxides: An infrared spectroscopic investigation
Author(s) -
Oertel Richard P.
Publication year - 1977
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.1977.360161017
Subject(s) - chemistry , stratum corneum , antiparallel (mathematics) , biophysics , conformational change , sulfoxide , keratin , protein secondary structure , beta sheet , crystallography , protein structure , biochemistry , organic chemistry , medicine , physics , pathology , quantum mechanics , magnetic field , biology
Formation of the antiparallel‐chain β‐sheet protein conformation is induced in in vitro human stratum corneum by three homologous organic sulfoxides known to enhance skin permeability: dimethylsulfoxide (Me 2 SO), hexylmethylsulfoxide (HxMeSO), and decylmethylsulfoxide (DecMeSO). Me 2 SO and HxMeSO apparently function by displacing water molecules bound to polar protein side‐chains, whereas DecMeSO probably interacts hydrophobically with the protein. The conformational transition does not result from lipid removal. The β‐sheet protein, most likely formed in normally α‐helical portions of the intracellular keratin filaments, is reconverted to α‐helix upon rehydration of the tissue. Though neat Me 2 SO produces the most β‐sheet of all treatments examined, the sequence of ability to promote β‐sheet formation at the 1 M level is HxMeSO > DecMeSO > Me 2 SO. Spectroscopic evidence is presented regarding the dependence of β‐sheet formation on sulfoxide concentration, treatment duration, pH, and tissue hydration. The relationship of this conformational change to the enhancement of skin permeability is briefly discussed. The result of sulfoxide treatment is different from results of sodium dodecylsulfate and heat treatments of stratum corneum.