Kinetically trapped self-assembly in synthetic nucleopeptides and nucleotides

Area of Science:

• Biochemistry
• Materials Science
• Molecular Biology

Background:

• Cellular functions often rely on thermodynamically unfavorable dynamic self-assembly processes.
• Understanding the principles governing self-assembly is crucial for biomimetic material design.

Purpose of the Study:

• To investigate the self-assembly behavior of a nucleopeptide with adenosine triphosphate (ATP) and its hydrolysis product, adenosine monophosphate (AMP).
• To explore the role of enzymatic hydrolysis in modulating self-assembled hydrogel formation and stability.

Main Methods:

• Formation of hydrogels using a nucleopeptide mixed with ATP.
• Testing hydrogel formation with the nucleopeptide and AMP.
• Enzymatic hydrolysis of ATP to AMP in situ using an ATPase enzyme within the nucleopeptide-AMP mixture.

Main Results:

• A self-assembled hydrogel was successfully formed from the nucleopeptide and ATP.
• The nucleopeptide and AMP mixture did not form a hydrogel under the same conditions.
• Upon enzymatic hydrolysis of ATP to AMP, the nucleopeptide-AMP system unexpectedly formed and maintained a self-assembled hydrogel, demonstrating kinetically trapped self-assembly.

Conclusions:

• Nucleopeptide-ATP interactions can lead to hydrogel formation.
• Enzymatic conversion of ATP to AMP can induce or stabilize self-assembled hydrogels through kinetic trapping.
• This finding reveals an unusual mechanism of self-assembly relevant to biological processes and materials science.