Noncovalent synthesis of protein dendrimers. Lempens, E. H M, van Baal, I., van Dongen, J. L J, Hackeng, T. M, Merkx, M., & Meijer, E W Chemistry, 15(35):8760–8767, Germany, September, 2009.
abstract   bibtex   
The covalent synthesis of complex biomolecular systems such as multivalent protein dendrimers often proceeds with low efficiency, thereby making alternative strategies based on noncovalent chemistry of high interest. Here, the synthesis of protein dendrimers using a strong but noncovalent interaction between a peptide and complementary protein is proposed as an efficient strategy to arrive at dendrimers fully functionalized with protein domains. The association of S-peptide to S-protein results in the formation of an active enzyme (ribonuclease S) and therefore serves as an ideal system to explore this synthetic approach. Native chemical ligation was used to couple four S-peptides by means of their C-terminal thioester to a cysteine-functionalized dendritic scaffold, thus yielding a tetravalent S-peptide wedge. A fully functional ribonuclease S tetramer was prepared by addition of four equivalents of S-protein. Biophysical techniques (isothermal titration calorimetry (ITC), surface plasmon resonance (SPR), and mass spectrometry) and an enzymatic activity assay were used to verify the formation of the multivalent complex. The noncovalent synthetic strategy presented here provides access to well-defined, dynamic, semisynthetic protein assemblies in high yield and is therefore of interest to the field of nanomedicine as well as biomaterials.
@ARTICLE{Lempens2009-xx,
  title    = "Noncovalent synthesis of protein dendrimers",
  author   = "Lempens, Edith H M and van Baal, Ingrid and van Dongen, Joost L J
              and Hackeng, Tilman M and Merkx, Maarten and Meijer, E W",
  abstract = "The covalent synthesis of complex biomolecular systems such as
              multivalent protein dendrimers often proceeds with low
              efficiency, thereby making alternative strategies based on
              noncovalent chemistry of high interest. Here, the synthesis of
              protein dendrimers using a strong but noncovalent interaction
              between a peptide and complementary protein is proposed as an
              efficient strategy to arrive at dendrimers fully functionalized
              with protein domains. The association of S-peptide to S-protein
              results in the formation of an active enzyme (ribonuclease S) and
              therefore serves as an ideal system to explore this synthetic
              approach. Native chemical ligation was used to couple four
              S-peptides by means of their C-terminal thioester to a
              cysteine-functionalized dendritic scaffold, thus yielding a
              tetravalent S-peptide wedge. A fully functional ribonuclease S
              tetramer was prepared by addition of four equivalents of
              S-protein. Biophysical techniques (isothermal titration
              calorimetry (ITC), surface plasmon resonance (SPR), and mass
              spectrometry) and an enzymatic activity assay were used to verify
              the formation of the multivalent complex. The noncovalent
              synthetic strategy presented here provides access to
              well-defined, dynamic, semisynthetic protein assemblies in high
              yield and is therefore of interest to the field of nanomedicine
              as well as biomaterials.",
  journal  = "Chemistry",
  volume   =  15,
  number   =  35,
  pages    = "8760--8767",
  month    =  sep,
  year     =  2009,
  address  = "Germany",
  language = "en"
}
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