Efficient one-pot cyclization/folding of Rhesus θ-defensin-1 (RTD-1)

Teshome L. Aboye, Yilong Li, Subhabrata Majumder, Jinfeng Hao, Alexander Shekhtman, Julio A. Camarero

Research output: Contribution to journalArticlepeer-review

22 Scopus citations

Abstract

We report an efficient approach for the chemical synthesis of Rhesus θ-defensin-1 (RTD-1) using Fmoc-based solid-phase peptide synthesis in combination with an intramolecular version of native chemical ligation. The corresponding linear thioester precursor was cyclized and folded in a one-pot reaction using reduced glutathione. The reaction was extremely efficiently yielding natively folded RTD-1 with minimal or no purification at all. This approach is fully compatible with the high throughput production of chemical libraries using this peptide scaffold.

Original languageEnglish (US)
Pages (from-to)2823-2826
Number of pages4
JournalBioorganic and Medicinal Chemistry Letters
Volume22
Issue number8
DOIs
StatePublished - Apr 15 2012

Bibliographical note

Funding Information:
This work was supported by National Institutes of Health Research Grant R01-GM090323 (J.A.C.) and NIH Grant 5R01GM085006-02 (A.S.); and by the Department of Defense Congressionally Directed Medical Research Program Grant PC09305 (J.A.C.).

Keywords

  • Antimicrobial peptide
  • Cyclic peptide
  • Defensin

Fingerprint Dive into the research topics of 'Efficient one-pot cyclization/folding of Rhesus θ-defensin-1 (RTD-1)'. Together they form a unique fingerprint.

Cite this