The study reveals that simple peptides can imitate the protection strategy of nature proteins

A new study by researchers from the Advanced Science Research Center of the Cuny Graduate Center (Cuny ASRC) reveals that extremely simple peptides can imitate a biological process that protects sensitive proteins from environmental stress.

The results, published in Nature materials, Offer a new promising approach to stabilize biomolecules such as vaccines and therapeutic proteins – potentially without needing refrigeration.

The study, led by Rein Ulijn, founding director of Cuny ASRC Nanoscience Initiative and distinguished chemistry professor at the Hunter College, shows how long three amino acids are – can undergo liquid -liquid proteins through a drying process that allows peptides to encapped it from proteins, to protect them and free Rehydration.

“Inspired by the way organizations like Tardigrades survive extreme dehydration, we asked if we could reproduce the nature strategy using minimum synthetic materials,” said Ulijn.

“To our surprise, we have found that simple tripeptides could form dynamic and reversible structures that protect proteins under stress. This opens up new possibilities for protein preservation.”

In biology, cells often react to stress by creating protection compartments through a process known as phases separation. These compartments stabilize vulnerable proteins and can dissolve again when the conditions improve.

The research team applied this principle to the design of adaptable materials based on peptides which imitate this process – offering a simple and effective alternative to conventional biomolecular stabilization methods, which often require complex formulations and logistics to the cold chain.

The main results of the study include:

• Tripeptides can form reversible disorderly assemblies which undergo phases separation during drying.
• These assemblies solidify in porous microparticles, effectively encapsulating proteins.
• During rehydration, peptides release their protein cargo with preserved structural integrity.
• The process imitates natural protection mechanisms and gives an overview of a new mode of training of supramolecular materials.

“This work not only reveals a new mechanism of self-organization of peptides, but also introduces a minimalist material platform for biotechnology applications,” said Ulijn.

The implications are of great range. From the distribution of vaccines to regions without reliable refrigeration to the new classes of intelligent and reactive materials, the study implements a fundamental work for practical innovations and additional scientific exploration.