Researchers Discover New Family of Simple Peptide that Form Stable Hydrogels

Published in Nature Chemistry

(New York, Dec. 9, 2014) _ New research has led to the discovery of a method that for the first time can help identify peptides that form simple, usable hydrogels. The study, published in Nature Chemistry, describes the new family of gels that can potentially be used in foods, cosmetics and biomedicine, and, due to their simplicity, may be manufactured at a low cost.

The discovery of the new method is the result of a collaborative project between the research groups of Dr. Rein V. Ulijn, the director of the Nanoscience Initiative at the new Advanced Science Research Center at the City University of New York, also a chemistry professor at Hunter College in the City University of New York, and Dr. Tell Tuttle, at the University of Strathclyde in Glasgow, Scotland.

Until now, there was no way to reliably predict whether a particular peptide sequence would have potential to form a gel. As a result, scientists relied on serendipity, conservative modification of known structures or conducting individual experiments of each sequence.

Peptides, the building blocks of living systems, also have tremendous potential as building blocks for new materials, including gels. But the large number of possible sequences makes it impossible to test all of them, limiting the potential for new applications.

Dr. Ulijn said, “Most people are familiar with the DNA as the code for life. This code translates into only 20 chemical building blocks – amino acids – that are combined in specific sequences, known as peptides, which provide the structures of living systems.

“The enormous number of sequences available from combinations of 20 amino acids harbors many interesting candidates, but it wasn’t possible to predict their material properties. We developed tools to predict the materials formed from 8,000 possible tripeptides.”

These tools led to the discovery of a new family of very simple tripeptides that are able to form a hydrogel at neutral pH. The study describes four examples of unprotected tripeptides that are able to form hydrogels. These peptides were discovered using the screening process described in the study.

“Our work describes four examples of unprotected tripeptides that are able to form hydrogels,” said Dr. Tuttle, who developed the computational approach for rapid screening of large peptide libraries. “The aim was to design structures based on peptides that are inspired by biology, yet much simpler, making them scalable, predictable and functional.”