Peptides are biomolecules formed when two or more amino acids that perform key functions in the human organism, such as hormones, neurotransmitters, painkillers and antibiotics, bind together. For this reason, they are much studied and used by the pharmaceutical industry, for example.
A study conducted by scientists in the Department of Biophysics at the Federal University of São Paulo’s Medical School (EPM-UNIFESP) in Brazil identified significant changes in the physicochemical properties of peptides during a spontaneous process of chemical change called pyroglutamination.
Pyroglutamination is a modification resulting from spontaneous conversion of glutamine to pyroglutamic acid, with a significant impact on the physical and chemical properties of peptides. It is a well-known but frequently overlooked part of peptide synthesis, and rarely explored in proteomics.
The researchers who conducted the study stress that it can occur rapidly and accelerates as temperature rises, underscoring the need for caution during laboratory experiments to prevent glutamine cyclization. It is especially important in conditions that mimic physiological environments where temperatures are in the range of 37° C, the normal temperature of a healthy human organism.
The discovery has implications for laboratory research and opens up new prospects for the study of neurodegenerative diseases such as Alzheimer’s and Parkinson’s, since after chemical modification the molecule acquires an amyloidal structure, which favors aggregation of molecules, forming plaques like those believed to cause the diseases