UNLABELLED UV resonance Raman spectroscopy (UVRRS) using 244-nm excitation was used to study the impact of aging on human dentin. The intensity of a spectroscopic feature from the peptide bonds in the collagen increases with tissue age, similar to a finding reported previously for human cortical bone. INTRODUCTION The structural changes that lead to compromised mechanical properties with age in dentin and bone are under intense study. However, in situ analyses of the content and distribution of the mineral phase are more highly developed at present than equivalent probes of the organic phase. MATERIALS AND METHODS Thirty-five human molars were divided into three groups: young/normal (23.3 +/- 3.8 years); aged/transparent (74.3 +/- 6.0 years), which had become transparent because of filling of the tubule lumens with mineral deposits; and aged/nontransparent (73.3 +/- 5.7 years). Control experiments were performed by demineralizing normal dentin. RESULTS Spectral features caused by both the amide backbone and resonance-enhanced side-chain vibrations were observed. This finding contrasts with reported Raman spectra of proteins in solution excited with similar UV wavelengths, where side chain vibrations, but not strong amide features, are observed. The strong intensity of the amide features observed from dentin is attributed to broadening of the resonance profile for the amide pi --> pi* transition caused by the environment of the collagen molecules in dentin. With increasing age, the height of one specific amide vibration (amide I) becomes significantly higher when comparing teeth from donors with an average age of 23 years to those of 73 years (p < 0.001). This trend of increasing amide I peak height with age is similar to that previously reported for human cortical bone. The amide I feature also increased in dentin that had been demineralized and dehydrated. CONCLUSIONS The similar trend of increasing amide I peak height with age in the UVRR spectra of both teeth and bone is surprising, given that only bone undergoes remodeling. However, by considering those observations together with this study of demineralized/dehydrated dentin and our prior work on dentin dehydrated with polar solvents, a consistent relationship between changes in the UVRR spectra and the collagen environment in the tissue can be developed.