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Peptide-Based Catalyst Mimicking Hydrolase Enzyme.

Kalpana Kumari1, Vivek Prakash1,2, Naveen Kumar1

  • 1Department of Biosciences and Bioengineering, Indian Institute of Technology Guwahati, Guwahati, Assam, India.

Journal of Peptide Science : an Official Publication of the European Peptide Society
|May 21, 2025
PubMed
Summary
This summary is machine-generated.

Researchers designed three peptide catalysts to mimic enzyme activity. Peptide P3 exhibited the highest catalytic activity, demonstrating that enzyme mimicry can be modulated by altering peptide sequence.

Keywords:
enzymeshydrolasekineticsnanofiberpeptide catalyst

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Area of Science:

  • Biochemistry
  • Nanotechnology
  • Catalysis

Background:

  • Peptide-based nanomolecular constructs are promising for creating enzyme mimics.
  • Designing artificial enzymes with tunable catalytic activity is a key challenge in molecular systems.

Purpose of the Study:

  • To design and evaluate tripeptide catalysts that mimic hydrolase enzymes.
  • To investigate the impact of histidine residue placement on catalytic activity.
  • To demonstrate the modulation of enzyme mimic activity through structural tuning.

Main Methods:

  • Synthesis of three Fmoc-tripeptide catalysts (P1, P2, P3) with varied histidine placement.
  • Assay of catalytic activity using a chromogenic substrate (p-nitrophenyl acetate).
  • Analysis of activity dependence on pH and temperature.

Main Results:

  • Peptide catalyst P3 demonstrated the highest hydrolytic activity towards p-nitrophenyl acetate.
  • Catalytic activity increased with rising pH and temperature.
  • Activity modulation was achieved by altering the tripeptide sequence.

Conclusions:

  • Tripeptide catalysts can effectively mimic hydrolase enzymes.
  • The position of key residues significantly influences catalytic efficiency.
  • This study validates the principle of modulating functional mimic activity by tuning molecular components.