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Synthesis and characterization of the 47‐residue heterodimeric antimicrobial peptide distinctin, featuring directed disulfide bridge formation
Author(s) -
Mullen Daniel G.,
Verardi Raffaello,
Porcelli Fernando,
Scaloni Andrea,
Barany George,
Veglia Gianluigi
Publication year - 2012
Publication title -
peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.22087
Subject(s) - chemistry , residue (chemistry) , disulfide bond , peptide , monomer , covalent bond , combinatorial chemistry , stereochemistry , biochemistry , organic chemistry , polymer
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. © 2012 Wiley Periodicals, Inc. Biopolymers (Pept Sci) 98: 479–484, 2012.