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Hierarchically Multivalent Peptide-Nanoparticle Architectures: A Systematic Approach to Engineer Surface Adhesion.

Woo-Jin Jeong1,2, Jiyoon Bu1, Roya Jafari3

  • 1Pharmaceutical Sciences Division and Wisconsin Center for NanoBioSystems (WisCNano), School of Pharmacy, University of Wisconsin-Madison, 777 Highland Ave, Madison, WI, 53705, USA.

Advanced Science (Weinheim, Baden-Wurttemberg, Germany)
|December 11, 2021
PubMed
Summary
This summary is machine-generated.

Researchers developed hierarchically multivalent architectures (HMAs) using peptide-conjugated dendrimers. This strategy enhances specific cell targeting by precisely controlling multivalent binding interactions.

Keywords:
binding aviditydendrimer-peptide conjugatehierarchically multivalent architecturesmultivalent bindingpeptide engineering

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Area of Science:

  • Biomaterials Science
  • Surface Chemistry
  • Molecular Engineering

Background:

  • Multivalent binding effects are crucial for modulating adhesion in biological and engineered systems.
  • Achieving precise control over strong avidity-based binding interactions remains a significant challenge.
  • Existing methods lack systematic strategies for stepwise enhancement of peptide multivalent binding.

Purpose of the Study:

  • To develop and test engineering strategies for systematically enhancing multivalent peptide binding.
  • To investigate the influence of linker length, peptide density, and surface arrangement on binding avidity.
  • To create optimized hierarchically multivalent architectures (HMAs) for enhanced cell targeting.

Main Methods:

  • Utilized poly(amidoamine) (PAMAM) dendrimers to create multivalent dendrimer-peptide conjugates (DPCs).
  • Engineered HMAs by varying poly(ethylene glycol) (PEG) linker lengths, peptide multiplicity per DPC, and surface arrangements.
  • Systematically evaluated the binding avidity and selectivity of different HMA configurations towards target cells.

Main Results:

  • Optimized HMA configurations demonstrated significantly enhanced target cell binding compared to control surfaces.
  • Achieved high selectivity in target cell binding through precise control of multivalent interactions.
  • Identified key parameters (PEG linkers, peptide density, surface arrangement) influencing binding avidity.

Conclusions:

  • The developed engineering strategies provide effective control over biomolecular multivalent interactions.
  • Hierarchically multivalent architectures (HMAs) offer a versatile platform for enhancing specific cell targeting.
  • These approaches can be applied individually or combined to guide the design of advanced biomaterials.