Given the current trend of longer life expectancy, there is an increasing need to maintain an optimal collagen levels during an even more extended lifespan. Due to a decrease in collagen levels after the age of 25 by approximately 2% per year, a person encounters many weakened body functions during the process of aging. Firstly, changes are visible in the form of skin wrinkles and its reduced elasticity, but later on various joint diseases (like arthritis), as well as mineralization and bone density disorders can develop. Currently, the most used method to increase collagen levels in the body is through collagen-based dietary supplements. The market offers a wide range of pharmaceutical collagen products derived from various animal (especially fish) sources. The aim of this research was to draw attention to a slightly different approach to maintaining collagen concentrations in the body, which could be much more effective in practice. Particularly, since the main reason for the decrease in the collagen level in the body is the increased collagen breakdown mediated by matrix metalloproteinases (MMP) enzymes, it is believed that inhibition of these enzymes would lead to a prevention of collagen breakdown in the body, thus preserving the level of endogenous collagen much during a much longer life expectancy. The existing research by Borkakoti et al. (1994) found a synthetic inhibitor that binds to the catalytic site of the human fibroblast collagenase enzyme and consequently prevents collagen degradation. This molecule showed good structural and ADMET properties, desirable in new drug development. Based on these findings, the goal of this research was to improve the binding of the inhibitor to the enzyme active site and thus to achieve a stronger inhibitory effect. Using molecular docking, the inhibitory effect of a total of 765 new molecules was predicted. The molecules were designed based on the model of the previously found synthetic inhibitor and adapted to the nature of amino acid residues in the active site of the enzyme. The research results show that ligands 157 and 303 have the best inhibitory effect on the tested enzyme with a binding energy of ΔG = –9.2 kcal mol-1, which is 2.8 kcal mol-1 lower than the binding energy of the initial synthetic inhibitor. However, the aforementioned two molecules exhibit slightly inferior pharmacokinetic properties than the initial synthetic inhibitor, with their toxicological profile being particularly concerning. The resulting molecules are worthy of further consideration due to the very favorable binding energy in the enzyme active site however, in order to be applicable in practice, they must undergo further optimization primarily of toxicological and then pharmacokinetic properties.