This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

2k9b

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Revision as of 07:32, 27 January 2022

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. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
NonStd Res:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[DDSK_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.

References

↑ 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
↑ 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
↑ 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
↑ 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
↑ 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

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2k9b"

@@ Line 3: / Line 3: @@
 <StructureSection load='2k9b' size='340' side='right'caption='[[2k9b]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2k9b]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2K9B OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2K9B FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2k9b]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2K9B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2K9B FirstGlance]. <br>
 </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=2k9b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2k9b OCA], [http://pdbe.org/2k9b PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2k9b RCSB], [http://www.ebi.ac.uk/pdbsum/2k9b PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2k9b ProSAT]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2k9b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2k9b OCA], [https://pdbe.org/2k9b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2k9b RCSB], [https://www.ebi.ac.uk/pdbsum/2k9b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2k9b ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/DDSK_PHYDS DDSK_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.<ref>PMID:10477123</ref> <ref>PMID:12379643</ref> <ref>PMID:17409003</ref> <ref>PMID:17442605</ref>
+[[https://www.uniprot.org/uniprot/DDSK_PHYDS DDSK_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.<ref>PMID:10477123</ref> <ref>PMID:12379643</ref> <ref>PMID:17409003</ref> <ref>PMID:17442605</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==

2k9b

From Proteopedia

Revision as of 07:32, 27 January 2022

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

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox