2k9b

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Structure and membrane interactions of the antibiotic peptide dermadistinctin K by multidimensional solution and oriented 15N and 31P solid-state NMR spectroscopy

Structural highlights

2k9b is a 1 chain structure with sequence from Phyllomedusa distincta. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Solution NMR, 20 models
Ligands:NH2
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

DRS1_PHYDS Has antibacterial activity against the Gram-positive bacteria S.aureus and E.faecalis, and the Gram-negative bacteria P.aeruginosa and E.coli. Has antiprotozoal activity against T.cruzi. Has antifungal activity against the yeasts C.tropicalis (MIC=10.1 uM), C.guilliermondii (MIC=20.3 uM), C.albicans (MIC=20.3 uM) and C.albicans ATCC 1023 (MIC=10.1 uM). Decreases viability of murine peritoneal cells. Fuses to, and disrupts liposomes.[1] [2] [3] [4]

Publication Abstract from PubMed

DD K, a peptide first isolated from the skin secretion of the Phyllomedusa distincta frog, has been prepared by solid-phase chemical peptide synthesis and its conformation was studied in trifluoroethanol/water as well as in the presence of sodium dodecyl sulfate and dodecylphosphocholine micelles or small unilamellar vesicles. Multidimensional solution NMR spectroscopy indicates an alpha-helical conformation in membrane environments starting at residue 7 and extending to the C-terminal carboxyamide. Furthermore, DD K has been labeled with (15)N at a single alanine position that is located within the helical core region of the sequence. When reconstituted into oriented phosphatidylcholine membranes the resulting (15)N solid-state NMR spectrum shows a well-defined helix alignment parallel to the membrane surface in excellent agreement with the amphipathic character of DD K. Proton-decoupled (31)P solid-state NMR spectroscopy indicates that the peptide creates a high level of disorder at the level of the phospholipid headgroup suggesting that DD K partitions into the bilayer where it severely disrupts membrane packing.

Structure and membrane interactions of the antibiotic peptide dermadistinctin K by multidimensional solution and oriented 15N and 31P solid-state NMR spectroscopy.,Verly RM, de Moraes CM, Resende JM, Aisenbrey C, Bemquerer MP, Pilo-Veloso D, Valente AP, Almeida FC, Bechinger B Biophys J. 2009 Mar 18;96(6):2194-203. PMID:19289046[5]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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Citations
3 reviews cite this structure
Insights into the mechanisms of action of host defence peptides from biophysical and structural investigations.
Bechinger et al. (2011)
2 more
18 other articles
No citations found

References

  1. ↑ Batista CV, da Silva LR, Sebben A, Scaloni A, Ferrara L, Paiva GR, Olamendi-Portugal T, Possani LD, Bloch C Jr. Antimicrobial peptides from the Brazilian frog Phyllomedusa distincta. Peptides. 1999;20(6):679-86. PMID:10477123
  2. ↑ Brand GD, Leite JR, Silva LP, Albuquerque S, Prates MV, Azevedo RB, Carregaro V, Silva JS, Sa VC, Brandao RA, Bloch C Jr. Dermaseptins from Phyllomedusa oreades and Phyllomedusa distincta. Anti-Trypanosoma cruzi activity without cytotoxicity to mammalian cells. J Biol Chem. 2002 Dec 20;277(51):49332-40. Epub 2002 Oct 11. PMID:12379643 doi:http://dx.doi.org/10.1074/jbc.M209289200
  3. ↑ Silva LP, Leite JR, Brand GD, Regis WB, Tedesco AC, Azevedo RB, Freitas SM, Bloch C Jr. Dermaseptins from Phyllomedusa oreades and Phyllomedusa distincta: liposomes fusion and/or lysis investigated by fluorescence and atomic force microscopy. Comp Biochem Physiol A Mol Integr Physiol. 2008 Nov;151(3):329-35. Epub 2007 Mar , 3. PMID:17409003 doi:http://dx.doi.org/10.1016/j.cbpa.2007.02.031
  4. ↑ Leite JR, Brand GD, Silva LP, Kuckelhaus SA, Bento WR, Araujo AL, Martins GR, Lazzari AM, Bloch C Jr. Dermaseptins from Phyllomedusa oreades and Phyllomedusa distincta: Secondary structure, antimicrobial activity, and mammalian cell toxicity. Comp Biochem Physiol A Mol Integr Physiol. 2008 Nov;151(3):336-43. Epub 2007 Mar , 20. PMID:17442605 doi:http://dx.doi.org/10.1016/j.cbpa.2007.03.016
  5. ↑ Verly RM, de Moraes CM, Resende JM, Aisenbrey C, Bemquerer MP, Pilo-Veloso D, Valente AP, Almeida FC, Bechinger B. Structure and membrane interactions of the antibiotic peptide dermadistinctin K by multidimensional solution and oriented 15N and 31P solid-state NMR spectroscopy. Biophys J. 2009 Mar 18;96(6):2194-203. PMID:19289046 doi:10.1016/j.bpj.2008.11.063

Contents


PDB ID 2k9b

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