Conjugating Catalytic Polyproline Fragments with a Self-Assembling Peptide Produces Efficient Artificial Hydrolases.

A polyproline fragment containing a catalytic dyad of His-His or Ser-His was coupled with a self-assembling peptide MAX1 to design new hydrolases (H2H5 and H2S5) for catalyzing ester hydrolysis. Circular dichroism measurements indicated that the peptides change their conformation from random coils to ß-sheets when pH increases from 5 to 10. IR spectra also displayed the vibration modes corresponding to their ß-structures at pH 9.0. Transmission electron microscopy (TEM) and atomic force microscopy (AFM) measurements showed that in solution, the designed peptides self-assemble into network fibrils having a significantly increased catalytic efficiency on ester hydrolysis. On p-nitrophenyl acetate (p-NPA) substrate, the designed peptides exhibit high catalytic efficiency at pH 9.0 (kcat/KM = 12.1 M-1 s-1 for H2H5, 13.3 M-1 s-1 for H2S5), and their efficiency is even better at pH 10.0 (kcat/KM = 24.3 M-1 s-1 for H2H5, 99.4 M-1 s-1 for H2S5). Additionally, H2H5 and H2S5 also display good activity on catalyzing the hydrolysis of p-nitrophenyl-(2-phenyl)-propanoate (p-NPP) and p-nitrophenyl methoxyacetate (p-NPMA). Combining the polyproline-based catalytic scaffold with a self-assembling peptide generates an efficient hydrolase, providing a new design for effective artificial enzymes.

Design of Polyproline-Based Catalysts for Ester Hydrolysis.

A number of simple oligopeptides have been recently developed as minimalistic catalysts for mimicking the activity and selectivity of natural proteases. Although the arrangement of amino acid residues in natural enzymes provides a strategy for designing artificial enzymes, creating catalysts with efficient binding and catalytic activity is still challenging. In this study, we used the polyproline scaffold and designed a series of 13-residue peptides with a catalytic dyad or triad incorporated to serve as artificial enzymes. Their catalytic efficiency on ester hydrolysis was evaluated by ultraviolet-visible spectroscopy using the p-nitrophenyl acetate assay, and their secondary structures were also characterized by circular dichroism spectroscopy. The results indicate that a well-formed polyproline II structure may result in a much higher catalytic efficiency. This is the first report to show that a functional dyad or triad engineered into a polyproline helix framework can enhance the catalytic activity on ester hydrolysis. Our study has also revealed the necessity of maintaining an ordered structure and a well-organized catalytic site for effective biocatalysts.

Efficacy = endowment x efficiency: revisiting efficacy and endowment effects in a public goods dilemma.

This article reexamines the efficacy and endowment effects in public good (PG) dilemma by conceptualizing that efficacy = endowment x efficiency. Endowment is the resource that a person can contribute. Efficiency is the impact of a unit of endowment. Efficacy is the total impact of contribution. The authors used a group project scenario to simulate a continuous contribution PG dilemma. The 2 x 2 x 2 x 2 experimental design manipulated own efficiency and own endowment as within-subject variables and the other persons' efficiency and endowment as between-subject variables. Results indicate that cooperation was mainly affected by one's endowment and others' efficiency. The authors distinguished among 3 types of efficiency effects: (a) an own-absolute-efficiency effect that efficient people put in more effort regardless of others' efficiency, (b) an other-absolute-inefficiency effect that people put in more effort when others are inefficient, and (c) a relative-inefficiency effect that inefficient people put in less effort in the presence of efficient people. Contrasting previous robust findings on efficiency, they identified a situation in which efficiency has no effects--when one has more endowment than do others.