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A Step Toward Creating Tiny Molecular Machines

Adenosine triphosphate (ATP) is often described as the energy currency of all life. It acts like a battery in cells, supplying energy for humans, animals, and plants. Now researchers from the Advanced Science Research Center at The Graduate Center, CUNY, have discovered a short peptide that is able to pair up with ATP. The study made the cover of ChemSystemsChem.

The study makes progress towards creating new materials to work as tiny molecular machines. These materials would help with chemical processes like emulsification, accelerating chemical reactions, and molecular recognition in industries from food science to biomedicine.

The cover of ChemSystemsChem shows artwork provided by the groups of Prof. Rein V. Ulijn at CUNY Advanced Science Research Center and Prof. Tell Tuttle at the University of Strathclyde. The image shows adenosine triphosphate, life’s ubiquitous energy source, interacting with a short peptide that was discovered using phage display. The formed complexes are dynamic and sample a shallow energy landscape.

The cover of ChemSystemsChem shows artwork provided by the groups of Prof. Rein V. Ulijn at CUNY Advanced Science Research Center and Prof. Tell Tuttle at the University of Strathclyde. The image shows adenosine triphosphate, life’s ubiquitous energy source, interacting with a short peptide that was discovered using phage display. The formed complexes are dynamic and sample a shallow energy landscape.

Ph.D. student Daniela Kroiss, ASRC research specialist Scott McPhee, and Professor Rein Ulijn of Hunter College and the ASRC were authors on the paper.

In using peptides to make active materials, researchers are taking a cue from nature. Peptides are chains of amino acids. Both peptides and their larger cousins, proteins, play numerous roles in living things, from signaling to connectivity and waste cleanup. With 20 standard amino acids to choose from and rearrange, scientists hope to design peptides to fill specific purposes.

The peptides will need fuel to do molecular work. So Kroiss and her collaborators looked to ATP.

While finding candidate peptides to build such materials has been a challenge in the past, the researchers overcame this by using a Nobel Prize-winning technique called phage display. The researchers screened about 100 million different heptapeptides (a peptide containing seven amino acids) to see if they could bind with ATP — and successfully identified one that does this well.

The authors say that by finding an ATP-binding peptide only seven amino acids long, the study also supports the hypothesis that short peptides could have been the evolutionary precursors of today’s larger proteins.

“Moreover, our results show that phage display is a powerful method that can be applied more widely to discover novel peptides that interact with small metabolites, such as ATP,” said Kroiss, who was lead author on the paper. “In the future, peptides identified using this technique could be used as building blocks for the design of active bio-inspired materials.”

Beyond SUM

Explore This Work

Unbiased Discovery of Dynamic Peptide‐ATP Complexes
ChemSystemsChem, 2019

Work By

Daniela Kroiss (Ph.D. Student, Biochemistry) | Profile 1
Rein Ulijn (Albert Einstein Professor of Chemistry, Biochemistry) | Profile 1 | Profile 2 | Profile 3