Editor’s note: This article is the first in a two-part series describing the anti-aging effects of a natural dipeptide. The first installment presents in vitro studies; the second considers clinical efficacy.
Peter T. Pugliese, MD, refers to elastin as “the youth protein” and boldly states that “there is probably no single protein that has as much to do with a person’s appearance and well-being as the protein elastin.” The skin’s elasticity and firmness are naturally maintained by a complex system of cross-linked proteins that strengthen the skin’s resistance to stretching. The most important protein structure for maintaining this system is the elastic fiber, which is made up mostly of elastin and associated proteins.
Historic research has indicated that elastin present in skin having undergone actinic elastosis shows changes in its amino acid composition; specifically, in its proportions of tyrosine (Tyr) and arginine (Arg). This, coupled with the fact that fragments of fibrillin-1 and fibulin-5 contain the sequence “Tyr-Arg,” and that triggering the coordinated synthesis of various proteins and enzymes is involved in the production of elastic fibers, led the authors to investigate the potential bioactivity of the natural dipeptide Kyotorphin (Tyr-Arg), albeit modified to N-Acetyl-Tyr-Arg-O-Hexadecyl Ester (NATAH).
The peptide N-Acetyl-Tyr-Arg-Hexadecylester (NATAH) was found to stimulate the synthesis of tropoelastin in cultured human dermal fibroblasts as well as augment the activity of all important actors in the assembly of elastic fibers, including Fibrillin 1, Fibulin 5, Decorin, LOX and Transglutaminase, among others. This is shown here both in monolayer cell cultures and in a 3D skin model.
This content is adapted from an article in GCI Magazine. The original version can be found here.