Total chemical synthesis of biologically active vascular endothelial growth factor.

Publication Type:

Journal Article

Authors:

Mandal, Kalyaneswar; Kent, Stephen B H

Source:

Angew Chem Int Ed Engl, Volume 50, Issue 35, p.8029-33 (2011)

Keywords:

Amino Acid Sequence, Chromatography, High Pressure Liquid, Crystallography, X-Ray, Dimerization, Mass Spectrometry, Molecular Sequence Data, Peptides, Protein Structure, Tertiary, Vascular Endothelial Growth Factor A

Abstract:

<p>Efficient access: the 204-residue covalent-dimer vascular endothelial growth factor with full mitogenic activity was prepared from three unprotected peptide segments by one-pot native chemical ligations. The covalent structure of the synthetic VEGF was confirmed by precise mass measurement, and the three-dimensional structure of the synthetic protein was determined by high-resolution X-ray crystallography.</p>