Comparative Analysis of Peptide Composition and Bioactivity of Different Collagen Hydrolysate Batches on Human Osteoarthritic Synoviocytes.

Collagen hydrolysates (CHs) are heterogeneous mixtures of collagen peptides that are often used as nutraceuticals for osteoarthritis (OA). In this study, we compared the peptide composition and pharmacological effects of three different CH preparations (CH-Alpha®, Peptan® B 2000 and Mobiforte®) as well as their production batches. Our biochemical analysis using MALDI-TOF mass spectrometry and the ICPL™-isotope labelling method revealed marked differences between different CH preparations and even between some production batches of the same preparation. We also investigated the pharmacological effects of these CHs on human fibroblast-like synoviocytes (FLS). No significant effects on cultured FLS could be demonstrated for either production batch of CH-Alpha®, Peptan® B 2000, and Mobiforte® analyzing a small number of pharmacological relevant targets. Thus, our study already shows for the first time that different production batches of the same CH preparation as well as different CH preparations can differ significantly in their peptide composition. In this line, further studies are also needed to verify equal pharmacological efficacy of CH batches on a much broader range of (patho)physiological relevant targets. If OA patients are to be offered a safe and effective nutraceutical a better knowledge about all potential effects as well as ensuring the same active-substance levels are a prerequisite.

Metabolic Response of Human Osteoarthritic Cartilage to Biochemically Characterized Collagen Hydrolysates.

The most frequent disease of the locomotor system is osteoarthritis (OA), which, as a chronic joint disease, might benefit more from nutrition than acute illnesses. Collagen hydrolysates (CHs) are peptidic mixtures that are often used as nutraceuticals for OA. Three CHs were characterized biochemically and pharmacologically. Our biophysical (MALDI-TOF-MS, NMR, AFM) and fluorescence assays revealed marked differences between CHs of fish (Peptan® F 5000, Peptan® F 2000) and porcine (Mobiforte®) origin with respect to the total number of peptides and common peptides between them. Using a novel dual radiolabeling procedure, no CH modulated collagen biosynthesis in human knee cartilage explants. Peptan® F 2000 enhanced the activities of the aggrecanase ADMATS4 and ADMATS5 in vitro without loss of proteoglycan from cartilage explants; the opposite effect was observed with Mobiforte®. Interleukin (IL)-6, matrix metalloproteinase (MMP)-1, -3 and -13 levels were elevated in explants that were treated with Mobiforte® and Peptan® F 5000, but not with Peptan® F 2000. In conclusion, the heterogeneous peptide composition and disparate pharmacological effects between CHs suggest that the effect of a CH preparation cannot be extrapolated to other formulations. Thus, the declaration of a CH as a safe and effective nutraceutical requires a thorough examination of its pleiotropic effects.