Collagen absorption bands in heated and rehydrated dentine.
The objective of this work is identifying changes in the collagen bands in heated and rehydrated dentine. We use bovine dentine slices that were heated in oven between 100 and 300 degrees C. The sample hydration was conducted in sodium chloride solution at 0.9 wt.%; the spectra were acquired by a Fourier transform infrared spectrometer in the spectral range of 4000-400 cm-1. Our results show a temperature range (T<or=175 degrees C) where the dentinal collagen can be partially denatured and reverted to initial conformation; a second region (175 degrees C<T<or=225 degrees C) where this process occurs partially and a third region (T>225 degrees C) where the collagen is denatured and no reversion is observed after rehydration. This work identifies an important characteristic that dentinal collagen can assume when the tissue is heated and rehydrated; these results indicate the denaturation temperature of dentinal collagen to be near 175-200 degrees C.
Bachmann
Luciano
L
Instituto de Ciências Exatas, Universidade Federal de Itajubá, Unifei, Avenida BPS, 1303 Pinheirinho, Itajubá, MG 37500-000, Brazil. bachmann@ipen.br
Gomes
Anderson S L
AS
Zezell
Denise M
DM
D000042:Absorption; D000818:Animals; D002417:Cattle; D003094:Collagen / Q000737:chemistry*; D003804:Dentin / Q000737:chemistry*; D006358:Hot Temperature; D011489:Protein Denaturation; D012965:Sodium Chloride; D013055:Spectrophotometry, Infrared; D017550:Spectroscopy, Fourier Transform Infrared; D014867:Water / Q000737:chemistry*
D014867:Water; D012965:Sodium Chloride; D003094:Collagen