Engineering a noncarrier to a highly efficient carrier peptide for noncovalently delivering biologically active proteins into human cells

Eric Mahlum, Deendayal Mandal, Chandralekha Halder, Avudaiappan Maran, Michael J. Yaszemski, Robert B. Jenkins, Mark E. Bolander, Gobinda Sarkar

Research output: Contribution to journalArticle

8 Scopus citations

Abstract

Noncovalent protein delivery into cells via peptide carriers is an emerging concept. Only a handful of such peptides are known. To address various limitations associated with protein delivery for therapeutic purposes, a greater number of different delivery peptides would be required. No general method exists for creating such peptides. By combining a sequence of 16 lysine residues (K16) with the signal peptide (SP) sequence of Kaposi's fibroblast growth factor (K-FGF), we have synthesized a peptide (K16SP) that efficiently and noncovalently delivers functionally intact proteins (immunoglobulin G molecules, β-galactosidase, and green fluorescent protein) into mammalian cells. The peptides K16 and SP each alone did not show any noncovalent protein-carrying capacity. K16SP appears to be nontoxic to cells and three to four times more efficient than a commercially available peptide reagent. Our approach offers proof-of-concept of a general strategy for creating a diverse array of peptide carriers for eventual therapeutic applications.

Original languageEnglish (US)
Pages (from-to)215-221
Number of pages7
JournalAnalytical Biochemistry
Volume365
Issue number2
DOIs
StatePublished - Jun 15 2007

Keywords

  • Noncovalent
  • Peptide carrier
  • Polylysine
  • Protein delivery
  • Signal peptide

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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