Synthesis and characterization of the 47-residue heterodimeric antimicrobial peptide distinctin, featuring directed disulfide bridge formation.

Daniel G. Mullen, Raffaello Verardi, Fernando Porcelli, Andrea Scaloni, George Barany, Gianluigi Veglia

Research output: Contribution to journalArticlepeer-review

4 Scopus citations

Abstract

Distinctin, a 47-residue heterodimeric peptide with potent antimicrobial activity, comprises two monomeric units linked covalently by a disulfide bond between Cys19 from the 22-residue A chain and Cys23 from the 25-residue B chain. Previous synthetic strategies involved assemblies of the two individual chains, followed by their co-oxidation to form the connecting disulfide bridge, and resulted in a mixture of three species: two homodimers and one heterodimer. Here, we report synthesis of exclusively heterodimeric distinctin, using recently developed tactics for directed disulfide bridge formation. Material prepared this way was characterized and found to be suitable for more detailed structural studies.

Original languageEnglish (US)
Pages (from-to)479-484
Number of pages6
JournalBiopolymers
Volume98
Issue number5
DOIs
StatePublished - 2012

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