Elasticity is the skin's ability to regain its shape after stretching or pressure. It is what distinguishes young skin—which "bounces back" quickly—from aging skin, where recovery is slower and incomplete. Behind this difference lies concrete biology, with names of proteins and processes that can be understood and, to some extent, influenced.
Collagen vs. Elastin: two proteins, the same function
Skin elasticity mainly depends on two proteins in the dermal extracellular matrix: collagen and elastin. Type I collagen provides mechanical resistance—it is the structure that prevents the skin from deforming excessively. Elastin is the protein that allows the skin to regain its original shape after deformation: it acts like a molecular spring. Both work together to define skin biomechanics.
Unlike collagen, which renews itself—though increasingly slowly with age—the elastin synthesized in childhood and adolescence is practically what we have for life. Adult fibroblasts produce very little new elastin. Therefore, once elastin fibers deteriorate due to UV damage, glycation, or oxidative stress, recovery is very limited. Preventing its deterioration is much more valuable than subsequent correction.
Why elasticity decreases with age
The loss of elasticity has multiple causes: progressive reduction in collagen synthesis by fibroblasts, deterioration of existing elastin fibers due to oxidative and enzymatic damage, glycation of both proteins making them more rigid, and reduction of hyaluronic acid content that acts as a support medium for the matrix. Menopause accelerates all these processes simultaneously.
What UV radiation, sugar, and tobacco do to collagen
The three external factors that most accelerate the loss of elasticity are well known: UV radiation (activates MMPs that degrade collagen and elastin, generates ROS that damage their structure), excessive sugar in the diet (causes glycation of protein fibers, making them rigid and difficult to renew), and tobacco (reduces blood flow to the dermis, generates oxidants that damage the extracellular matrix and activates degradative enzymes). Avoiding or reducing these factors has a direct and documented impact on the preservation of elasticity.
Can oral collagen improve elasticity? The studies
The answer is yes, with nuances. Clinical studies with hydrolyzed collagen peptides show measurable improvements in skin elasticity with continued use. The proposed mechanism is twofold: absorbed bioactive peptides (especially Pro-Hyp and Hyp-Gly) stimulate endogenous synthesis of collagen and hyaluronic acid in dermal fibroblasts, and activate the production of the LOX protein (lysyl oxidase), which is the enzyme responsible for the cross-linking that gives resistance to collagen fibers.
Peptan® and clinical studies with measurable parameters
The study by Proksch et al. (Skin Pharmacology and Physiology, 2014) evaluated the effect of 2.5 g/day of Peptan® collagen peptides in 69 women aged 35 to 55 years for 8 weeks. The results showed a statistically significant improvement in skin elasticity (measured with a cutometer) in the active group compared to placebo. The study by Schunck et al. (2015) with 114 women aged 45 to 65 documented a 20% reduction in periorbital wrinkle depth after 8 weeks.
LEVIAL's dosage—8,000 mg of Peptan® per vial—is well above the doses evaluated in these studies, ensuring a functionally relevant load of bioactive peptides.
How long until changes are observed: realistic expectations
Studies indicate measurable improvements from 4-8 weeks, with more consolidated results at 12 weeks. This implies that three months of continuous use is the minimum reasonable timeframe for an honest evaluation of the results. Collagen biology does not work in days. The expectation of "I'll notice the difference in a week" has no scientific backing and should be a red flag, not a sign of trust, for any product that uses it.
