2M2Y: Solution structure of the antimicrobial peptide Btd-2[3,4]

theta-Defensins are ribosomally synthesized cyclic peptides found in the leukocytes of some primate species and have promising applications as antimicrobial agents and scaffolds for peptide drugs. The cyclic cystine ladder motif, comprising a cyclic peptide backbone and three parallel disulfide bonds, is characteristic of theta-defensins. In this study, we explore the role of the cyclic peptide backbone and cystine ladder in the structure, stability, and activity of theta-defensins. theta-Defensin analogues with different numbers and combinations of disulfide bonds were synthesized and characterized in terms of their NMR solution structures, serum and thermal stabilities, and their antibacterial and membrane-binding activities. Whereas the structures and stabilities of the peptides were primarily dependent on the number and position of the disulfide bonds, their antibacterial and membrane-binding properties were dependent on the cyclic backbone. The results provide insights into the mechanism of action of theta-defensins and illustrate the potential of theta-defensin analogues as scaffolds for peptide drug design.
PDB ID: 2M2YDownload
MMDB ID: 107846
PDB Deposition Date: 2013/1/3
Updated in MMDB: 2013/07
Experimental Method:
solution nmr
Similar Structures:
Biological Unit for 2M2Y: monomeric; determined by author
Molecular Components in 2M2Y
Label Count Molecule
Protein (1 molecule)
Molecule annotation
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