Total chemical synthesis of the B1 domain of protein L from Peptostreptococcus magnus.


Journal Article

Reported here is a native chemical ligation strategy for the total chemical synthesis of the B1 domain of protein L. A synthetic construct of this 76 amino acid protein domain was prepared by the chemoselective ligation of two unprotected polypeptide fragments, one containing an N-terminal cysteine residue and one containing a C-terminal thioester moiety. The polypeptide fragments utilized in the ligation reaction were readily prepared by stepwise solid phase peptide synthesis (SPPS) methods for Boc-chemistry. The milligram quantities of protein required for conventional biophysical studies were readily accessible using the synthetic protocol described here. The folding properties of the synthetic protein L construct were also determined and found to be very similar to those of a similar wild-type protein L constructs prepared by recombinant-DNA methods. This work facilitates future unnatural amino acid mutagenesis experiments on this model protein system to further dissect the molecular basis of its folding and stability.

Full Text

Duke Authors

Cited Authors

  • Yang, X; Fitzgerald, MC

Published Date

  • June 2006

Published In

Volume / Issue

  • 34 / 3

Start / End Page

  • 131 - 141

PubMed ID

  • 16690101

Pubmed Central ID

  • 16690101

Electronic International Standard Serial Number (EISSN)

  • 1090-2120

International Standard Serial Number (ISSN)

  • 0045-2068

Digital Object Identifier (DOI)

  • 10.1016/j.bioorg.2006.02.001


  • eng