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Intrinsically Disordered Proteins02:18

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Intrinsically disordered proteins are a group of proteins that do not fold into specific three-dimensional structures. Their structural flexibility allows them to complement ordered proteins to perform functions that are inaccessible to rigid structures. They are more common in eukaryotes than prokaryotes and may either be exclusively intrinsically disordered or hybrid proteins, consisting of a mix of ordered and disordered regions. The absence of a rigid structure in these proteins can be...
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Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a...
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Context-Dependent Heterotypic Assemblies of Intrinsically Disordered Peptides.

Yuchen Qiao1, Ayisha Zia2, Grace Wu1

  • 1Department of Chemistry, Brandeis University, 415 South St., Waltham, Massachusetts 02454, United States.

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Intrinsically disordered peptides (IDPs) can form nanofibers through context-dependent assembly. This study reveals how charged IDPs with aromatic segments self-assemble into novel nanomaterials.

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Area of Science:

  • Biochemistry
  • Materials Science
  • Nanotechnology

Background:

  • Intrinsically disordered regions (IDRs) are crucial for protein function but often neglected in peptide assembly design.
  • Context-dependent interactions, driven by other molecules, govern protein behavior.

Purpose of the Study:

  • To exploit IDRs for context-dependent heterotypic assembly of intrinsically disordered peptides.
  • To design adaptive, multifunctional peptide nanomaterials using IDPs.

Main Methods:

  • Attaching aromatic segments to oppositely charged intrinsically disordered peptides.
  • Utilizing cryo-electron microscopy (Cryo-EM) for structural analysis.
  • Investigating post-assembly morphological changes via controlled peptide addition.

Main Results:

  • Oppositely charged peptides formed heterotypic nanofibers, while same-charged peptides did not self-assemble.
  • Cryo-EM revealed a β-sheet core, conformational heterogeneity, and a disorder-to-order continuum.
  • Post-assembly addition of charged peptides induced morphological changes, forming bundles, dependent on aromatic residue content.

Conclusions:

  • Demonstrated context-dependent self-assembly of intrinsically disordered peptides.
  • Provided atomistic insights into heterotypic intrinsically disordered peptide assemblies.
  • Showcased a straightforward method for designing adaptive peptide nanomaterials.