Publication: Structural studies of β-hairpin peptidomimetic antibiotics that target LptD in Pseudomonas sp
Structural studies of β-hairpin peptidomimetic antibiotics that target LptD in Pseudomonas sp
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Schmidt, J., Patora-Komisarska, K., Moehle, K., Obrecht, D., & Robinson, J. A. (2013). Structural studies of β-hairpin peptidomimetic antibiotics that target LptD in Pseudomonas sp. Bioorganic & Medicinal Chemistry, 21(18), 5806–5810. https://doi.org/10.1016/j.bmc.2013.07.013
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Abstract
We report structural studies in aqueous solution on backbone cyclic peptides that possess potent antimicrobial activity specifically against Pseudomonas sp. The peptides target the β-barrel outer membrane protein LptD, which plays an essential role in lipopolysaccharide transport to the outer membrane. The peptide L27-11 contains a 12-residue loop (T(1)W(2)L(3)K(4)K(5)R(6)R(7)W(8)K(9)K(10)A(11)K(12)) linked to a DPro-LPro template. Two related peptides were also studied, one with various Lys to ornithine or diaminobutyric acid substit
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- Schmidt, Jasmin
- Patora-Komisarska, Kristina
- Moehle, Kerstin
- Obrecht, Daniel
- Robinson, John A
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Schmidt, J., Patora-Komisarska, K., Moehle, K., Obrecht, D., & Robinson, J. A. (2013). Structural studies of β-hairpin peptidomimetic antibiotics that target LptD in Pseudomonas sp. Bioorganic & Medicinal Chemistry, 21(18), 5806–5810. https://doi.org/10.1016/j.bmc.2013.07.013
