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

Spatially resolved infrared (IR) and Raman images are acquired from human hair cross sections or intact hair fibers. The full informational content of these spectra are spatially correlated to hair chemistry, anatomy, and structural organization through univariate and multivariate data analysis. Specific IR and Raman images from untreated human hair describing the spatial dependence of lipid and protein distribution, protein secondary structure, lipid chain conformational order, and distribution of disulfide cross-links in hair protein are presented in this study. Factor analysis of the image plane acquired with IR microscopy in hair sections, permits delineation of specific micro-regions within the hair. These data indicate that both IR and Raman imaging of molecular structural changes in a specific region of hair will prove to be valuable tools in the understanding of hair structure, physiology, and the effect of various stresses upon its integrity.

Raman microspectroscopic and dynamic vapor sorption characterization of hydration in collagen and dermal tissue.

Water is an integral part of collagen's triple helical and higher order structure. Studies of model triple helical peptides have revealed the presence of repetitive intrachain, interchain, and intermolecular water bridges (Bella et al., Structure 1995, 15, 893-906). In addition, an extended cylinder of hydration is thought to be responsible for collagen fiber assembly. Confocal Raman spectroscopy and dynamic vapor sorption (DVS) measurements of human Type I collagen and pigskin dermis were performed to probe relative humidity (RH)-dependent differences in the nature and level of collagen hydration. Raman spectra were also acquired as a function of time for both Type I collagen and pigskin dermis samples upon exchange of a 100% RH H(2) O to deuterium oxide (D(2) O) environment. Alterations in Amide I and III modes were consistent with anticipated changes in hydrogen bonding strength as RH increased and upon H → D exchange. Of note is the identification of a Raman spectral marker (band at 938 cm(-1) ) which appears to be sensitive to alterations in collagen-bound water. Analysis of DVS isotherms provided a quantitative measure of adsorbed and absorbed water vapor consistent with the Raman results. The development of a Raman spectral marker of collagen hydration in intact tissue is relevant to diverse fields of study ranging from the evaluation of therapeutics for wound healing to hydration of aging skin.