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Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides
07:26

Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides

Published on: November 21, 2013

Sequence, structure, and function of peptide self-assembled monolayers.

Ann K Nowinski1, Fang Sun, Andrew D White

  • 1Department of Chemical Engineering, University of Washington, Seattle, Washington 98195, USA.

Journal of the American Chemical Society
|March 10, 2012
PubMed
Summary
This summary is machine-generated.

A four-residue linker (-PPPPC) improves peptide self-assembled monolayers (SAMs) on gold, creating well-ordered structures and reducing protein adsorption. This offers a simpler alternative to poly(ethylene glycol) for controlling cell adhesion.

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Solid-phase Submonomer Synthesis of Peptoid Polymers and their Self-Assembly into Highly-Ordered Nanosheets

Published on: November 2, 2011

Area of Science:

  • Biomaterials Science
  • Surface Chemistry
  • Nanotechnology

Background:

  • Cysteine is a common choice for attaching peptides to gold surfaces.
  • Peptide self-assembled monolayers (SAMs) are crucial for various surface functionalization applications.
  • Achieving well-ordered SAMs with high surface density is essential for optimal performance.

Purpose of the Study:

  • To investigate the impact of a rigid, hydrophobic four-residue linker (-PPPPC) on peptide SAM structure and function.
  • To compare the performance of a peptide with the -PPPPC linker (EKEKEKE-PPPPC-Am) against a cysteine-terminated peptide (EKEKEKE-C-Am).
  • To evaluate the potential of the -PPPPC linker for controlling specific cell adhesion without using poly(ethylene glycol).

Main Methods:

  • Circular dichroism (CD) spectroscopy
  • Attenuated total internal reflection Fourier transform infrared (ATR-FTIR) spectroscopy
  • Molecular dynamics (MD) simulations
  • Surface plasmon resonance (SPR) sensing
  • X-ray photoelectron spectroscopy (XPS)

Main Results:

  • The -PPPPC linker facilitated the formation of well-ordered peptide SAMs with secondary structures, unlike the random structures formed by cysteine-terminated peptides.
  • Peptides with the -PPPPC linker exhibited significantly lower and more consistent protein adsorption compared to cysteine-terminated peptides.
  • XPS confirmed strong gold-thiol binding for both peptide types, attributing the functional differences to SAM structure.
  • The -PPPPC linker demonstrated superior performance over shorter linkers (-PC, -PPC, -PPPC).
  • The functionalized peptide (EKEKEKE-PPPPC-Am) with an RGD sequence enabled controlled specific cell adhesion.

Conclusions:

  • The inclusion of a rigid, hydrophobic four-residue linker (-PPPPC) is a superior strategy for creating well-ordered and dense peptide SAMs on gold surfaces.
  • This linker strategy enhances the nonfouling properties of peptide surfaces and offers a viable alternative to traditional methods for controlling cell adhesion.
  • The -PPPPC linker provides a versatile platform for peptide-based surface engineering, avoiding complex chemistries.