A seminal paper has resulted from this work that comes from Rein Ulijn, a CUNY professor at Hunter College. As the longtime leader of the CUNY ASRC Nanoscience Initiative, he’s found that short, simple peptides can work wonders at replicating nature’s techniques for shielding proteins. Their research, published on August 5, 2025, discloses a thrilling discovery. Even very short peptides, of only three amino acids, are able to effectively encapsulate and protect proteins when subjected to the stress of drying and rehydration. This finding has far-reaching consequences for the field of biotech and the wide-scale preservation of proteins.
This study provides evidence that these short peptides experience LLPS. This process allows them to wrap themselves around proteins to form protective diamonds. Using an unconventional drying process, these custom made peptides can form cages around proteins that preserve them even in torturous conditions. When protein is rehydrated, the proteins are released whole, demonstrating the success of this novel approach.
The Mechanism Behind Peptide Self-Organization
Ulijn’s research has helped to uncover a de novo mechanism for peptide self-organization. This discovery may unlock exciting new directions in biotechnology. The study’s findings underscore how these simple tripeptides can form dynamic, reversible structures that effectively shield proteins from environmental stress.
“This work not only reveals a novel mechanism of peptide self-organization but also introduces a minimalistic material platform for applications in biotechnology,” – Ulijn.
This novel mechanism was modeled after nature’s toughest creatures, including tardigrades, which can survive even the most deadly desiccation. Ulijn emphasizes the importance of their work’s namesake natural phenomenon in shaping their research focus.
“Inspired by how organisms like tardigrades survive extreme dehydration, we asked whether we could replicate nature’s strategy using minimal synthetic materials,” – Ulijn.
This property means that these peptides can encapsulate proteins, and this biocompatibility and stability could change the game in protein storage and preservation. This breakthrough is particularly important in industries that require permanence in extreme environments.
Imaging the Innovation
An electron microscopy image captured by Sheng Zhang shows the results of Ulijn’s research. The above image shows an assortment of porous spheres and half-dome particles that were produced via the evaporation of a peptide solution. This illustrative image reaffirms the report’s findings. It serves to demonstrate the kind of organic structural complexity possible with relatively simple synthetic materials.
This picture does an awesome job of illustrating how these peptides form protective matrices around proteins. It allows researchers to better understand how to use them to their fullest potential.
Implications for Biotechnology
Simple, designer peptides can do a great job encapsulating proteins. This advance opens up exciting new opportunities for drug delivery and enzyme stabilization for biotechnology applications.
“To our surprise, we found that simple tripeptides could form dynamic, reversible structures that protect proteins under stress. This opens up new possibilities for protein preservation,” – Ulijn.
The scientific community has shown great interest in the possible applications of these peptides and are continuing to make new discoveries. Ulijn’s work shows the amazing power of marrying natural strategies to synthetic creativity.