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Related Experiment Video

Updated: Jun 4, 2026

Bacterial Peptide Display for the Selection of Novel Biotinylating Enzymes
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An unusual cell penetrating peptide identified using a plasmid display-based functional selection platform.

Shan Gao1, Melissa J Simon, Christopher D Hue

  • 1Department of Chemical Engineering, Columbia University, New York, New York 10027, USA.

ACS Chemical Biology
|February 5, 2011
PubMed
Summary

Researchers discovered a novel cell-penetrating peptide (CPP), SG3, using plasmid display. This peptide efficiently delivers cargo like green fluorescent protein (GFP) into cells, even when not highly cationic, offering new possibilities for gene and drug delivery.

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Area of Science:

  • Biotechnology and Molecular Biology
  • Drug Delivery Systems
  • Peptide Chemistry

Background:

  • Cell-penetrating peptides (CPPs) are crucial for intracellular delivery of therapeutic molecules.
  • Identifying novel CPPs with specific functionalities from large peptide libraries is a significant challenge.
  • Existing CPPs often rely on high cationic charge, limiting their application scope.

Purpose of the Study:

  • To discover novel cell-penetrating peptides (CPPs) with unique properties from a randomized peptide library.
  • To evaluate the efficacy of a newly identified peptide (SG3) in delivering cargo, such as green fluorescent protein (GFP).
  • To demonstrate the utility of the plasmid display (PD) platform for identifying functional CPPs.

Main Methods:

  • Utilized a functional selection system based on plasmid display (PD) to screen a 14-mer peptide library.

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  • Conducted four rounds of screening using PC12 cells.
  • Tested identified peptides for their ability to deliver GFP and fused SG3 to a pro-apoptotic BH3 peptide.

    • Main Results:

    • Identified a novel CPP, designated SG3, which exhibits cell-penetrating properties but is not highly cationic.
    • In the presence of cationic lipid (Lipofectamine2000), SG3 significantly outperformed the TAT CPP in delivering GFP to PC12 cells and primary astrocytes.
    • Fusion of SG3 to a BH3 peptide induced significant cell death in primary astrocytes, confirming intracellular delivery of functional cargo.

    Conclusions:

    • The plasmid display platform is effective for discovering novel CPPs with unique capabilities from randomized libraries.
    • The SG3 peptide represents a promising new CPP with potential for gene and drug delivery applications, particularly due to its non-cationic nature.
    • This discovery expands the toolkit for intracellular delivery strategies in biomedical research and therapeutics.