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j. Soc. Cosmet. Chem., 42, 35-44 (January/February 1991) Relationship between collagen hydrolysate molecular weight and peptide substantivity to hair GILBERT R. MINTZ, GALE M. REINHART, and BRUCE LENT, CalBiochem Corporation, La Jolla, CA 92037 (G.R.M.), Revlon, Edison, NJ (G.M.R.), and VideoJet Systems, Inc., Chicago, iL (B.L.). Received October 1990. Synopsis Cosmetic grade collagen hydrolysates were incubated with virgin (natural) and bleached/waved (damaged) hair tresses. The bound collagen peptides were removed by both a high-temperature (50øC) and a high-salt (0.5 M NaCI) soak. As much as four times more fluorescamine reactive and hydroxyproline-containing peptides are removed from damaged than from natural hair. Gel filtration shows differences in the molec- ular weight (MW) distribution of peptides present in the high-temperature and high-salt soakings. These results demonstrate two distinct types of proteins that bind to hair: high-molecular-weight (30,000 daltons) and low-molecular-weight (1,000 to 3,000 daltons). The majority of the hydroxyproline-con- taining peptides •at bind to bleached/waved hair is in the lower molecular weight range and is probably composed of more basic amino acids. INTRODUCTION Previous studies indicate that cosmetic grade protein hydrolysates are complex mixtures of various molecular weight (MW) polypeptides (1). The capacity of a substance to absorb/adsorb to a surface is referred to as substantivity. The substantive nature of collagen-derived peptides to human hair has been demonstrated (2-4). Typically, pep- tide substantivity has been shown by monitoring the presence of the amino acid hy- droxyproline (which is a component of collagen but absent in hair) absorbed on hair after a series of water rinsings to remove non-specific peptides. Radiolabeling studies have demonstrated that small quantities of amino acids (5) and alkyl-dimethyl quater- nary derivatives of hydrolyzed collagen peptides (4) are absorbed to hair. In all of the studies to date, no information is available on the selective removal and subsequent characterization of peptides from the complex hydrolysates applied to hair. Methods used to manufacture protein hydrolysates typically yield a broad MW distribution of peptides (1,000-30,000 daltons). Accordingly, it was of interest to characterize the collagen peptides that were removed from the protein hydrolysate solution by specifi- cally binding to the hair. We have extended previous observations regarding the binding of collagen protein hy- drolysates (peptides) to hair by characterizing the MW of the hydroxyproline-con- 35