Cell‐Penetrating Peptide Fusion Proteins

Muñoz-Alarcón, Andrés; Helmfors, Henrik; Karlsson, Kristin; Langel, Ülo

doi:10.1002/9781118354599.ch26

Search citation statements

Order By: Relevance

Paper Sections

Select...

Discussion1

Citation Types

Supporting

Mentioning

Contrasting

Year Published

2017

2018

Publication Types

Select...

Article2

Relationship

Self Cite0

Independent2

Authors

Journals

Cited by 2 publications

(1 citation statement)

References 137 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…As new applications of Cas9 emerge, there is a growing necessity for the development of new methods for the safe and efficient delivery of the Cas9 ribonucleoprotein inside living cells. 18 Despite having shown great efficiency for the transport of other functional proteins, 40 , 41 cell-penetrating peptides have not been described in the supramolecular delivery of the Cas9 ribonucleoprotein. The report by Ramakrishna et al required the fusion of the cationic polyarginine to the C-terminal Cys introduced in the Sp Cas9 sequence.…”

Section: Discussionmentioning

confidence: 99%

Peptide/Cas9 nanostructures for ribonucleoprotein cell membrane transport and gene edition

et al. 2017

View full text Add to dashboard Cite

show abstract

Section: Discussionmentioning

confidence: 99%

Peptide/Cas9 nanostructures for ribonucleoprotein cell membrane transport and gene edition

et al. 2017

View full text Add to dashboard Cite

show abstract

Supramolecular Recognition and Selective Protein Uptake by Peptide Hybrids

Juanes

Lostalé‐Seijo

Granja

et al. 2018

Chemistry A European J

View full text Add to dashboard Cite

The intracellular transport of exogenous proteins has emerged as one of the most promising methodologies for biotechnology and chemical biology. Currently, protein delivery is mainly achieved by liposome encapsulation, translational fusion, and ionic/hydrophobic non-covalent aggregation with transporting molecular vehicles. This work introduces the concept of supramolecular recognition and selective transport of proteins by peptide hybrid materials. A helical amphiphilic cationic peptide that bears two orthogonal alkoxyamines for the precise anchoring of protein ligands has been designed. After the attachment of these protein ligands, the peptide showed a high binding affinity for its target protein (i.e., mannose/Concanavalin A, Biotin/Streptavidin). The resulting peptide/protein hybrids were taken up by human cells such as HeLa and HepG2. The concept described in this manuscript could potentially be adapted, through the appropriate choice of ligands, to the transport of other proteins with suitable supramolecular binding motifs.

show abstract

Cell‐Penetrating Peptide Fusion Proteins

Cited by 2 publications

References 137 publications

Peptide/Cas9 nanostructures for ribonucleoprotein cell membrane transport and gene edition

Peptide/Cas9 nanostructures for ribonucleoprotein cell membrane transport and gene edition

Supramolecular Recognition and Selective Protein Uptake by Peptide Hybrids

Contact Info

Product

Resources

About