Protein conformational changes induced in human stratum corneum by organic sulfoxides: An infrared spectroscopic investigation

Abstract

SynopsisFormation of the antiparallel-chain @-sheet protein conformation is induced in in uitro human stratum corneum by three homologous organic sulfoxides known to enhance skin permeability: dimethylsulfoxide (MeZSO), hexylmethylsulfoxide (HxMeSO), and decylmethylsulfoxide (DecMeSO). MeZSO 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 @-sheet protein, most likely formed in normally a-helical portions of the intracellular keratin filaments, is reconverted to a-helix upon rehydration of the tissue. Though neat Me&O produces the most @-sheet of all treatments examined, the sequence of ability to promote @-sheet formation at the 1M level is HxMeSO > DecMeSO > MefiO. Spectroscopic evidence is presented regarding the dependence of @-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.

Er:YAG laser treatments on dentine surface: micro-Raman spectroscopy and SEM analysis

“…In the inset is shown the typical Raman signal from protein component of dentine, from which the plotted data have been evaluated, by a procedure of peak deconvolution. 13,14 In our case the short pulse laser treatment seems to increase the defects in the collagen component of dentine with respect to those occurring in long pulse laser and mechanical treated surfaces, in spite of the observed reduction of the band width of CH 2 symmetrical vibration component. This behaviour can be explained by a size reduction of collagen components consistently with the observed reduction of intensity.…”

Measuring changes in chemistry, composition, and molecular structure within hair fibers by infrared and Raman spectroscopic imaging

“…Both are very sensitive protein conformation and correlations between the frequencies of Amides I and II and protein secondary structures are well documented for different types of keratin. 14 The current work extends the investigation of keratin to different hair regions by adding spatial resolution within the hair. Thus, in the spectrum obtained from cortex shown in Fig.…”

Effect of Penetration Enhancer DMSO on In-Vitro Skin Permeation of Acyclovir Transdermal Microemulsion Formulation.

“…Studies performed over40 years ago on healthy volunteers painted with 90%DMSO twice daily for 3 weeks resulted in erythema, scaling, contact uticaria, stinging and burning sensations and several volunteers developed systemic symptoms [25]. DMSO is widely used to denature pro application to human skin has been shown to change the intercellular keratin confirmation, from a helical to β sheet [26,27]. As well as an effect on the proteins, DMSO has also been shown to interact with the intercellular lipid domains of human stratum corneum.…”