New method for site-specific modification of liposomes with proteins using sortase A-mediated transpeptidation

Bioconjug Chem. 2012 Mar 21;23(3):650-5. doi: 10.1021/bc200694t. Epub 2012 Mar 8.


A new method was developed for site-specific modifications of liposomes by proteins via sortase A (SrtA)-mediated transpeptidation reactions. In this regard, the enhanced green fluorescent protein (eGFP) was biologically engineered to carry at its polypeptide C-terminus the LPATG motif recognized by SrtA and used as the protein donor for linking to liposomes that were decorated with phospholipids carrying a diglycine motif as the other SrtA substrate and the eGFP acceptor. Under the influence of SrtA, eGFP was efficiently attached to liposomes, as proved by analyzing the enzymatic reaction products and the resultant fluorescent liposomes. It was observed that increasing the concentration and the distance of the diglycine motif on and from the liposome surface could significantly improve the efficiency of liposome modification by proteins. It is anticipated that this strategy can be widely useful for the modification of liposomes by other proteins.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Aminoacyltransferases / chemistry*
  • Bacterial Proteins / chemistry*
  • Base Sequence
  • Cysteine Endopeptidases / chemistry*
  • DNA Primers
  • Liposomes*
  • Magnetic Resonance Spectroscopy
  • Mass Spectrometry
  • Peptides / chemistry*
  • Proteins / chemistry*


  • Bacterial Proteins
  • DNA Primers
  • Liposomes
  • Peptides
  • Proteins
  • Aminoacyltransferases
  • sortase A
  • Cysteine Endopeptidases