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Synthesis of Information-bearing Peptoids and their Sequence-directed Dynamic Covalent Self-assembly
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Sequence Changes Modulate Peptoid Self-Association in Water.

Amelia A Fuller1, Christian J Jimenez1, Ella K Martinetto1

  • 1Department of Chemistry & Biochemistry, Santa Clara University, Santa Clara, CA, United States.

Frontiers in Chemistry
|May 12, 2020
PubMed
Summary
This summary is machine-generated.

Researchers engineered water-soluble peptoids, N-substituted glycine oligomers, to adopt specific structures. Sequence modifications were found to alter peptoid self-assembly and structural organization in aqueous solutions.

Keywords:
circular dichroism (CD) spectroscopyfluorescence spectroscopypeptidomimeticpeptoidself-associationsize exclusion chromatography

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Area of Science:

  • Supramolecular Chemistry
  • Polymer Chemistry
  • Biomaterials Science

Background:

  • Peptoids, N-substituted glycine oligomers, are versatile peptidomimetics.
  • Engineering peptoids for regular secondary and tertiary structures is crucial for emulating peptide functions.
  • Understanding sequence-structure relationships in water-soluble peptoids remains an underdeveloped area.

Purpose of the Study:

  • To investigate how sequence modifications influence the structural features of water-soluble peptoids.
  • To design and synthesize novel peptoid variants with naphthalene-functionalized side chains.
  • To provide insights for designing water-soluble peptoids with predictable higher-order structures.

Main Methods:

  • Design and synthesis of five 15-residue water-soluble peptoids.
  • Structural evaluation using circular dichroism spectroscopy.
  • Analysis of self-assembly and conformational flexibility via fluorescence spectroscopy and size exclusion chromatography.

Main Results:

  • Sequence alterations successfully modulated peptoid conformational flexibility and amphiphilicity.
  • Spectral data confirmed that sequence changes impact the degree of peptoid assembly in aqueous solutions.
  • The organization of self-assembled peptoid structures was demonstrably affected by sequence variations.

Conclusions:

  • Sequence design is a critical factor in controlling the structural properties of water-soluble peptoids.
  • This study provides foundational knowledge for creating peptoids with defined secondary and tertiary structures.
  • The findings will guide the development of advanced peptoid-based materials with tailored functionalities.