One of the most critical functions for cellular health is proper protein folding . When a protein is synthesized, it must adopt a specific three-dimensional shape to be functional. This process is neither automatic nor foolproof: it requires the help of specialized molecules called molecular chaperones , also known as chaperone proteins .

Chaperones act as cellular supervisors of protein folding . They temporarily bind to newly formed or misfolded proteins, stabilizing them, preventing them from aggregating or becoming toxic, and guiding them toward their correct functional structure. In other words, they are responsible for maintaining proteostasis , the quality and functionality of the cellular protein environment.

The role of chaperones in aging

Throughout life, our cells synthesize millions of proteins. However, over time, folding efficiency decreases, and chaperones become less active or abundant. This leads to an accumulation of misfolded or partially damaged proteins, which can:

• Form insoluble aggregates that alter cellular function.

• Inhibit critical physiological processes.

• Activate inflammatory responses and cellular stress.

This deterioration has been identified as one of the factors driving age-related diseases, especially those of the central nervous system. In Alzheimer's, for example, chaperones fail to control the abnormal folding of proteins such as beta-amyloid or tau, which contributes to the formation of neurotoxic plaques.

Main chaperone families

• HSPs (Heat Shock Proteins) : These are the best known and most studied. They are induced under conditions of thermal, oxidative, or inflammatory stress, and help refold denatured proteins or direct them toward degradation.

• HSP70 and HSP90 : They actively participate in preventing protein collapse in aging cells.

• Chaperonins : Large multiprotein complexes that facilitate folding into closed compartments within the cell.

With aging, the expression of these proteins decreases and their functionality is compromised, paving the way for a more vulnerable cellular environment.

Is it possible to stimulate the action of chaperones through nutrition?

Yes. Scientific literature shows that certain natural compounds and nutrients can induce the expression of chaperone proteins or enhance their activity. Some of the most relevant are:

• Curcumin , the active ingredient in Curcuma Sevens , has been shown to induce the expression of HSP70 and HSP27, reinforcing the cellular response to thermal and oxidative stress.

• Omega-3 , present in Omega 3 Sevens , improves the fluidity of cell membranes and the homeostasis of the endoplasmic reticulum, a key site where many chaperones act.

• Plant polyphenols such as resveratrol or EGCG from green tea, which although not included in the Sevens line (yet...), are dietary supplements known for their ability to modulate cellular stress pathways.

• Magnesium , in Magnesium Sevens , is involved in the functioning of enzymes that collaborate with chaperones in the management of misfolded proteins.

• B vitamins , such as those present in Sevens Multivitamins , contribute to maintaining an energy metabolism and a redox environment compatible with the efficient work of chaperones.

Additional stimulation through hormetic stress

The concept of hormesis refers to controlled exposure to certain levels of stress (such as physical exercise, cold, heat, or fasting) that induce an adaptive response in the body. One of the most consistent responses to these stimuli is the increased expression of chaperone proteins, as part of the cellular defense system.

Conclusion

Chaperone proteins are essential for preserving the functional integrity of the cell. They act silently, correcting protein folding errors and preventing the formation of harmful aggregates. As we age, their activity declines, but we can stimulate their action through dietary strategies, appropriate supplementation, and habits that promote controlled cellular stress. In this sense, Sevens products represent a complementary support for maintaining the activity of these cellular guardians of protein balance.