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Structuring Peptide Dendrimers through pH Modulation and Substrate Binding.

Luís C S Filipe1, Sara R R Campos1, Miguel Machuqueiro2

  • 1Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa , Av. da República, EAN, 2780-157 Oeiras, Portugal.

The Journal of Physical Chemistry. B
|September 3, 2016
PubMed
Summary
This summary is machine-generated.

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pH significantly influences the structure of higher-generation peptide dendrimers by altering protonation states. These pH-induced conformational changes are crucial for understanding dendrimer function and designing new pH-responsive systems.

Area of Science:

  • Supramolecular Chemistry
  • Computational Chemistry
  • Biomaterials Science

Background:

  • Dendrimers are synthetic macromolecules with unique branched structures.
  • pH and electrostatic interactions critically affect dendrimer conformation and function.
  • Previous computational studies have not fully explored pH-dependent protonation equilibria in dendrimers.

Purpose of the Study:

  • To investigate the impact of pH on the protonation and conformational behavior of peptide dendrimers.
  • To analyze the relationship between protonation, conformation, and catalytic activity.
  • To understand dendrimer-substrate interactions at the molecular level.

Main Methods:

  • Constant-pH molecular dynamics (MD) simulations were performed for peptide dendrimers of generations 1-4.

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  • Simulations were conducted at various pH values, including the optimal catalytic pH.
  • Dendrimer-substrate interactions were simulated using MD.

    • Main Results:

    • Lower generation dendrimers (1-2) showed minimal structural response to pH changes.
    • Higher generation dendrimers (3-4) exhibited significant pH-dependent structural organization.
    • Protonation-conformation coupling modulated intramolecular interactions and overall dendrimer shape.
    • Dendrimer-substrate interactions restricted conformational flexibility and promoted homogeneity via hydrogen bonds and ion pairs.

    Conclusions:

    • pH plays a critical structuring role in higher-generation peptide dendrimers, influencing their conformation and function.
    • Understanding pH-dependent protonation is key to designing advanced, tunable dendritic systems.
    • Dendrimer-substrate interactions stabilize specific conformations, enhancing catalytic efficiency.