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Related Concept Videos

Peptide Bonds02:43

Peptide Bonds

75.9K
A peptide bond covalently attaches amino acids through a dehydration reaction. One amino acid's carboxyl group and another amino acid's amino group combine, releasing a water molecule. The resulting bond is the peptide bond. The products that such linkages form are peptides. As more amino acids join this growing chain, the resulting chain is a polypeptide. Each polypeptide has a free amino group at one end. This end has the N-terminal, or the amino-terminal, and the other end has a free...
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Synthesis of Information-bearing Peptoids and their Sequence-directed Dynamic Covalent Self-assembly
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A Reversibly Porous Supramolecular Peptide Framework.

Dominic F Brightwell1, Giada Truccolo1, Kushal Samanta1

  • 1Supramolecular Interfacial and Synthetic Chemistry Group, School of Physical Sciences, Ingram Building, University of Kent, CT2 7NH, Canterbury, UK.

Chemistry (Weinheim an Der Bergstrasse, Germany)
|August 30, 2022
PubMed
Summary

Researchers created the first supramolecular peptide framework (SPF) using a polyproline helix. This novel helical peptide self-assembly exhibits dynamic porosity and enantioselective guest inclusion.

Keywords:
enantioselectivityhelical structureshost-guest systemspeptidespolyprolinesupramolecular chemistry

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Area of Science:

  • Supramolecular Chemistry
  • Materials Science
  • Biomaterials Engineering

Background:

  • Bio-inspired building blocks are crucial for developing novel supramolecular frameworks.
  • Self-assembly of peptides into ordered structures is a key area of research.

Purpose of the Study:

  • To present the first polyproline helix self-assembled into a supramolecular peptide framework (SPF).
  • To demonstrate the framework's properties, including dynamic porosity and enantioselective guest inclusion.

Main Methods:

  • Utilizing a short oligoproline adopting the polyproline II conformation.
  • Driving self-assembly through hydrogen-bonding and dispersion interactions.
  • Investigating thermal activation and guest-induced effects on porosity.

Main Results:

  • Successfully formed a reversibly porous, crystalline supramolecular peptide framework (SPF).
  • Demonstrated thermal activation leading to dynamic porosity.
  • Showcased enantioselective guest inclusion within the framework.

Conclusions:

  • The polyproline helix serves as a novel building block for supramolecular peptide frameworks.
  • The demonstrated self-assembly principles can guide the design of future peptide-based frameworks.
  • This work opens avenues for developing advanced metal-peptide frameworks.