ArticleBiopolymers2012
Synthesis and characterization of the 47-residue heterodimeric antimicrobial peptide distinctin, featuring directed disulfide bridge formation.
Article in Biopolymers, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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Who cites it
1 citing paper in PubMed.
- Solution-phase-peptide synthesis via the group-assisted purification (GAP) chemistry without using chromatography and recrystallization.Chemical communications (Cambridge, England) · 2014Article
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Authors and funding
6 authors.
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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.
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