title: Ligand-Receptor Interaction Modulates the Energy Landscape of Enzyme-Instructed Self-Assembly of Small Molecules.
abstract: The concurrence of enzymatic reaction and ligand-receptor interactions is common for proteins, but rare for small molecules and has yet to be explored. Here we show that ligand-receptor interaction modulates the morphology of molecular assemblies formed by enzyme-instructed assembly of small molecules. While the absence of ligand-receptor interaction allows enzymatic dephosphorylation of a precursor to generate the hydrogelator that self-assembles to form long nanofibers, the presence of the ligand-receptor interaction biases the pathway to form precipitous aggregates containing short nanofibers. While the hydrogelators self-assemble to form nanofibers or nanoribbons that are unable to bind with the ligand (i.e., vancomycin), the addition of surfactant breaks up the assemblies to restore the ligand-receptor interaction. In addition, an excess amount of the ligands can disrupt the nanofibers and result in the precipitates. As the first example of the use of ligand-receptor interaction to modulate the kinetics of enzymatic self-assembly, this work not only provides a solution to evaluate the interaction between aggregates and target molecules but also offers new insight for understanding the emergent behavior of sophisticated molecular systems having multiple and parallel processes.
authors: Department of Chemistry, Brandeis University , 415 South Street, MS 015, Waltham, Massachusetts 02453, United States.
authors: Richard
authors: R
authors: Haburcak
authors: Department of Chemistry, Brandeis University , 415 South Street, MS 015, Waltham, Massachusetts 02453, United States.
authors: Junfeng
authors: J
authors: Shi
authors: Department of Chemistry, Brandeis University , 415 South Street, MS 015, Waltham, Massachusetts 02453, United States.
authors: Xuewen
authors: X
authors: Du
authors: Department of Chemistry, Brandeis University , 415 South Street, MS 015, Waltham, Massachusetts 02453, United States.
authors: Dan
authors: D
authors: Yuan
authors: Department of Chemistry, Brandeis University , 415 South Street, MS 015, Waltham, Massachusetts 02453, United States.
authors: Bing
authors: B
authors: Xu
mesh_terms: D000469:Alkaline Phosphatase / Q000737:chemistry / Q000378:metabolism*; D055162:Biocatalysis; D007700:Kinetics; D008024:Ligands; D010316:Particle Size; D054852:Small Molecule Libraries / Q000737:chemistry / Q000378:metabolism*; D013499:Surface Properties; D013501:Surface-Active Agents / Q000737:chemistry / Q000378:metabolism; D014640:Vancomycin / Q000737:chemistry / Q000378:metabolism*
chemical_list: D008024:Ligands; D054852:Small Molecule Libraries; D013501:Surface-Active Agents; D014640:Vancomycin; D000469:Alkaline Phosphatase