Role of melanin and artificial hair color in preventing photo‐oxidative damage to hair
Authors: Ruetsch S.B. , Yang B. , Kamath Y.K. 
Published: September 2004

This research is a multifaceted study which investigates not only the role of melanin in providing photostability to natural hair color and hair proteins, but also the claim that the presence of specific artificial colors in hair slows down the rate of photodegradation of hair proteins. In earlier studies, the extractability of protein from photodegraded hair was investigated and showed that many of the cleaved proteins could not be extracted because of photo‐oxidative cross‐linking. The current study investigates the effect of the amount of melanin in hair of different ethnicity and the presence of artificial hair colors on the extractability of the main classes of hair proteins. Furthermore, the data are used in the interpretation of the effect of these components in being able to prevent photo‐oxidative damage to hair proteins.

When exposed to sunlight, hair undergoes changes in chemical, mechanical and morphological properties. The UVB and UVA regions of the solar spectrum are the most damaging to human hair. Of these two, the UVA region is predominant in the solar spectrum at low altitudes. Hair of different ethnicity responds differently to the damaging radiation of the solar spectrum, because of different amounts of melanin present in hair. Melanin absorbs the impinging radiation (especially at the lower wavelengths (254–350 nm), and converts it by some complex internal mechanism into heat. Because of this, melanin provides a photochemical protection to natural hair color and hair proteins and prevents their photodegradation. However, the melanin pigments act sacrificially and become themselves degraded in the process of protecting the proteins from light. As a result, this «protective» effect of the melanin pigments does not last during long‐term intense exposure, when, regardless of the amount of melanin in hair, most matrix, intermediate filament and high molecular weight hair proteins undergo photo‐oxidative cross‐linking into higher molecular weight species, and their extractability from hair decreases significantly.

The goal of this study is to demonstrate how UV‐radiation affects natural and artificial hair color during long‐term exposures. Bright‐field and UV‐microspectrophotometry and an electrophoretic separation technique (SDS‐PAGE) were chosen as investigative techniques for these studies, because they are well‐suited to accurately and reproducibly investigate the initial properties of a specific hair sample and the changes in these properties as a result of long‐term light‐exposure. The goal of this paper is not to relate this to the content and type of melanin in hair. Electrophoresis, while not measuring the exact quantitative amount of protein extracted, is a semi‐quantitative method, where increases in brightness of the bands represent increased amounts of proteins that were extracted of that specific protein from hair. This electrophoretic study attempts to determine whether the presence of natural or artificial color in hair influences the protein extractability in unaltered hair and the photo‐oxidative cross‐linking during light‐exposure.

The bright‐field microspectrophotometric study showed that high concentrations of melanin provide protection to the melanin itself and that they prevent loss of natural hair color during light‐exposure. However, neither large amounts of melanin in hair of different ethnicity, nor artificial hair colors (even a dye with an absorption in the UV region) provide protection to the hair proteins against photodegradation under the conditions used in this study.

UV‐microspectrophotometry has suggested the formation of high levels of photo‐oxidized proteins as a result of light‐exposure. Electrophoresis revealed photo‐oxidative cross‐linking of most matrix, intermediate filament and high molecular weight hair proteins into their higher molecular weight analogues, rendering them less extractable due to their lowered diffusivity. Only very low levels of low molecular weight matrix proteins could be extracted.