Science & Research

Mechanism of Action

As one of the most widely researched collagen peptides on the market, Nippi Collagen is supported by a notable amount of scientific evidence. Clinical research into collagen peptide benefits began over 40 years ago and has expanded over the past decade. The results are a compelling body of scientific substantiation. Collagen’s benefits, bioavailability and efficacy have been demonstrated in double-blind, placebo-controlled clinical studies and published in leading scientific journals.

Studies support that collagen peptides extracted from fish consist of small peptide molecules that have a superior bioavailability and digestibility compared to other collagen products.

Due to lower molecular weight, it is absorbed at a higher level through the intestinal barrier into the bloodstream and carried throughout the body, leading to collagen synthesis in the joint tissues, bones and skin dermis.

Nippi Collagen Efficacy Demonstrated in Scientific Studies

Collagen peptides from marine sources have an amino acid composition that reveals a higher concentration of glycine, proline and hydroxyproline, which can be detected in the blood after ingestion. Protein is mostly digested and absorbed as amino acids. Glycine represents about one-third of the amino acid in collagen peptides and is known to play various roles, including functioning as a neurotransmitter. It is also a precursor for synthesis of heme and glutathione, as well as proteins in the body.

Clinical research has shown collagen to be partly absorbed in peptide form. For instance, the dipeptide prolyl-hydroxyproline (Pro-Hyp) is the main peptide component appearing in the body after collagen peptide ingestion. This specific dipeptide was reported to increase the number and the growth of cells spreading from skin in studies done on mice. Peptides resulting from collagen digestion are also chemoattractants for fibroblasts and may play a part in the stimulation of those cells that synthesize new collagen fibers (Shigemura, et al.). Collagen degradation peptides might attract these cells and result in repair of damaged tissue (Dybba, et al.).

Furthermore, growth of these cells was also enhanced significantly by Pro-Hyp. These studies suggest that ingested collagen peptide exhibits its effects on health through mechanisms unique to collagen peptides. Consequently, collagen has unique properties that are not found in other proteins, and these properties may be the reason for the effects of collagen peptide ingestion on bones, joints, skin, hair and nails. 

Excellent Absorption and Digestibility

Results confirm that collagen is effectively absorbed into the blood. Several in vivo studies demonstrate the high bioavailability of collagen peptides with the use of marker collagen peptides. When present in the blood, collagen peptides will efficiently reach the target tissues, where they act as building blocks for the cells and help boost the production of new collagen fibers.

Nippi Collagen is also at the forefront of new research on Nippi Collagen. The studies listed below were selected from many references to give evidence of the wide range of published investigations and clinical research that can be found on collagen’s mechanism of action (MOA).

Science Review

Ichikawa S, et al. Hydroxyproline-containing dipeptides and tripeptides quantified at high concentration in human blood after oral administration of gelatin hydrolysate. Int J Food Sci Nutr. 2010;61(1):52–60.

Iwai K, et al. Identification of food-derived collagen peptides in human blood after oral ingestion of gelatin hydrolysates. J Agric Food Chem. 2005;53:6531–6536.

Laskin DL, Kimura T, Sakakibara S, Riley DJ, Berg RA. Chemotactic activity of collagen-like polypeptides for human peripheral blood neutrophils. J Luekocyte Biol. 1986;39:255–266.

Mano H. Action mechanism of collagen peptide on bone, cartilage and joint. 1st Symp collagen peptide, Tokyo, Japan, 2009.

Postlethwaite AE, Kang A. Collagen and collagen peptide-induced chemotaxis of human blood monocytes. J Exp Med. 1976;143:1299–1307.

Postlethwaite AE, Seyer JM, Kang AH. Chemotactic attraction of human fibroblasts to type I, II, and III collagens and collagen-derived peptides. Proc Natl Acad Sci USA. 1978;75:871–875.

Prockop DJ, Keiser HR, Sjoerdsma A. Gastrointestinal absorption and renal excretion of hydroxyproline peptides. Lancet. 1962;2:527–528.

Ratnayake WMN, et al. Influence of dietary protein and fat on serum lipids and metabolism of essential fatty acids in rats. Br J Nutr. 1997;78:459–467.

Rose ML, et al. Dietary glycine inhibits the growth of B16 melanoma tumors in mice. Carcinogenesis. 1999;30:793–798.

Shigemura Y, et al. Effect of prolyl-hydroxyproline (Pro-Hyp), a food-derived collagen peptide in human blood, on growth of fibroblasts from mouse skin. J Agric Food Chem. 2009;57:444–449.

Shigemura Y, Sato K. Ann Meet Jap Soc Biosci Biotechnol Agrochem, 2008 (Kansai div).

Yin M, et al. Glycine accelerates recovery from alcohol-induced liver injury. J Pharmacol Exp Ther. 1998;286:1014–1019.

Nippi Collagen’s efficacy is demonstrated in scientific studies.
Contact us for more information on Nippi Collagen clinical studies.