2008
DOI: 10.1155/2008/109782
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Penetration mechanism of dimethyl sulfoxide in human and pig ear skin: An ATR–FTIR and near-FT Raman spectroscopicin vivoandin vitrostudy

Abstract: The penetration mechanism of dimethyl sulfoxide (DMSO) in human skinin vivoandin vitroand pig ear skin in vitro was studied using attenuated total reflectance (ATR) Fourier transform (FT) infrared (IR) and near-FT-Raman spectroscopy. The results showed changes in the conformation of the skin keratins from an α-helical to a β-sheet conformation. These changes were proved to depend on the concentration of free water in the sample as DMSO tended to bind to free water before the protein-bound water was replaced an… Show more

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Cited by 20 publications
(23 citation statements)
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“…The first and the second band can be attributed to the α -helix and β -sheet structure, respectively. 46,47 The fact that the band at ~20° for the regenerated KER (purple curve) has the same intensity as that of the wool, but at ~9° it has only a broad shoulder instead of a pronounced band as in wool seems to indicate that regenerated KER has relatively lower α -helix contain and higher β -sheet, β -turn and random structure than wool. Similarly, the structure of two KER composites (25:75 CS:KER and 25:75 CEL:KER (green and blue curve)) is more similar to regenerated KER than wool, namely, relatively lower α -helix and higher β -sheet, β -turn and random structure.…”
Section: Resultsmentioning
confidence: 99%
“…The first and the second band can be attributed to the α -helix and β -sheet structure, respectively. 46,47 The fact that the band at ~20° for the regenerated KER (purple curve) has the same intensity as that of the wool, but at ~9° it has only a broad shoulder instead of a pronounced band as in wool seems to indicate that regenerated KER has relatively lower α -helix contain and higher β -sheet, β -turn and random structure than wool. Similarly, the structure of two KER composites (25:75 CS:KER and 25:75 CEL:KER (green and blue curve)) is more similar to regenerated KER than wool, namely, relatively lower α -helix and higher β -sheet, β -turn and random structure.…”
Section: Resultsmentioning
confidence: 99%
“…[31][32][33] Dimethyl sulfoxide has been shown to change keratin conformation and also interact with SC lipids. 34,35) However, the interactions of these CPEs with SC lipids was mainly on the polar head region. 34,36,37) Therefore, low fluidity in the hydrophobic chain of SCLL lipids was observed in our study.…”
Section: Discussionmentioning
confidence: 99%
“…The amide I band provides information about the secondary structure of proteins in the skin [27]. An α-helix protein conformation gives rise to a band in the range of 1647 -1657 cm -1 while a β-sheet structure is associated with the 1621 -1640 cm -1 and 1671 -1679 cm -1 regions [28]. A shoulder near 1620 -1630 cm -1 was observed for both PG-and DMSO-treated samples.…”
Section: Atr-ftir Spectra For Tape Stripping Workmentioning
confidence: 99%