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Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
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Switchable Zinc(II)-Responsive Globular β-Sheet Peptide.

Truc Lam Pham1,2, Michael Kovermann3, Franziska Thomas1,2

  • 1Institute of Organic Chemistry, Heidelberg University, Im Neuenheimer Feld 270, 69120 Heidelberg, Germany.

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|December 22, 2021
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Summary
This summary is machine-generated.

Researchers developed a novel peptide that changes shape upon binding zinc ions. This pH-switchable beta-sheet peptide acts as a mini-receptor, offering potential for new biomaterials.

Keywords:
WW domainpH-switchprotein engineeringreceptorzinc switch

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Materials Science

Background:

  • Protein function relies on conformational changes influenced by environmental factors.
  • Developing synthetic peptides that mimic protein conformational switching is crucial for biomimetic applications.

Purpose of the Study:

  • To engineer a small, monomeric beta-sheet peptide capable of switching between molten globule and folded states.
  • To investigate the role of zinc(II) ion binding in inducing conformational changes.
  • To characterize the pH-switchable properties and stability of the engineered peptide.

Main Methods:

  • Peptide design with a His3-site for metal ion coordination.
  • Zinc(II) binding assays to determine affinity and specificity.
  • Circular Dichroism (CD) and multinuclear Nuclear Magnetic Resonance (NMR) spectroscopy for structural characterization.
  • pH-titration studies to assess switchability and stability.

Main Results:

  • The peptide specifically binds Zn(II) in the low micromolar range, reversibly switching conformation.
  • The His3-site facilitates Zn(II) recognition over other divalent metal ions.
  • The peptide exhibits robust pH-switchable behavior around pKa 6 and stability through multiple cycles.
  • Structural analysis confirmed the conformational transition upon Zn(II) binding.

Conclusions:

  • A synthetic beta-sheet peptide was successfully designed to undergo reversible conformational changes upon Zn(II) binding.
  • This peptide demonstrates tunable and stable switching behavior, making it a promising prototype for Zn(II) mini-receptors.
  • The findings present a viable strategy for creating responsive biomimetic materials.