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2ojm

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Revision as of 07:51, 2 March 2022

Solution structure and cell selectivity of Piscidin 1 and its analogues

Structural highlights

2ojm is a 1 chain structure. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	2ojn, 2ojo
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[MORO_MORSA] Exhibits broad spectrum antimicrobial activity against Gram-positive and Gram-negative bacteria as well as against a variety of fungi. Has hemolytic activity. Seems to disrupt the membranes by adopting an alpha helical conformation and forming toroidal pores.^[1] ^[2]

Publication Abstract from PubMed

Piscidin 1 (Pis-1) is a novel cytotoxic peptide with a cationic alpha-helical structure that was isolated from the mast cells of hybrid striped bass [Silphaduang, U., and Noga, E. J. (2001) Nature 414, 268-269]. Pis-1 is not selective for bacterial versus mammalian cells. In the present study, to develop novel antibiotic peptides with selectivity for bacterial cells, we examined the effect of substituting two glycine residues, Gly8 and Gly13, with Ala or Pro on this peptide's structure and biological activities. The bacterial cell selectivity of the peptides decreased in the following order: Gly-->Pro analogues > Gly-->Pro/Ala analogues > Pis-1 > Gly-->Ala analogues. The antimicrobial and hemolytic activities and abilities to permeabilize the model phospholipid membranes were higher for Pis-1 with Gly or Pro at position 8 than for its counterparts with either Gly or Pro at position 13. We determined the tertiary structure of Pis-1 and its analogues in the presence of SDS micelles by NMR spectroscopy. We found that Pis-1 has an alpha-helical structure from Phe2 to Thr21. Also, Pis-1 AA (Gly8, Gly13-->Ala8, Ala13) with higher antibacterial and hemolytic activity than Pis-1 has a stable alpha-helical structure from Phe2 to Thr21. Pis-1 PG (Gly-->Pro8) with bacterial cell selectivity has a hinge structure at Pro8, which provides flexibility in piscidin, followed by a three-turn helix from Val10 to Gly22 in the C-terminal region. Taken together, our results demonstrate that the conformational flexibility provided by introduction of a Pro at position 8, coupled with the primary anchoring of phenylalanines and histidines in the N-terminus to the cell membrane and the optimal length of the C-terminal amphipathic alpha-helix, are the critical factors that confer antibacterial activity and bacterial cell selectivity to Pis-1 PG. Pis-1 PG may be a good candidate for the development of a new drug with potent antibacterial activity but without cytotoxicity.

Solution structure and cell selectivity of piscidin 1 and its analogues.,Lee SA, Kim YK, Lim SS, Zhu WL, Ko H, Shin SY, Hahm KS, Kim Y Biochemistry. 2007 Mar 27;46(12):3653-63. Epub 2007 Mar 1. PMID:17328560^[3]

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

References

↑ Silphaduang U, Noga EJ. Peptide antibiotics in mast cells of fish. Nature. 2001 Nov 15;414(6861):268-9. PMID:11713517 doi:http://dx.doi.org/10.1038/35104690
↑ Campagna S, Saint N, Molle G, Aumelas A. Structure and mechanism of action of the antimicrobial peptide piscidin. Biochemistry. 2007 Feb 20;46(7):1771-8. Epub 2007 Jan 25. PMID:17253775 doi:10.1021/bi0620297
↑ Lee SA, Kim YK, Lim SS, Zhu WL, Ko H, Shin SY, Hahm KS, Kim Y. Solution structure and cell selectivity of piscidin 1 and its analogues. Biochemistry. 2007 Mar 27;46(12):3653-63. Epub 2007 Mar 1. PMID:17328560 doi:10.1021/bi062233u

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/2ojm"

@@ Line 3: / Line 3: @@
 <StructureSection load='2ojm' size='340' side='right'caption='[[2ojm]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2ojm]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OJM OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2OJM FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2ojm]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OJM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2OJM FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2ojn|2ojn]], [[2ojo|2ojo]]</td></tr>
+</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2ojn|2ojn]], [[2ojo|2ojo]]</div></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=2ojm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ojm OCA], [http://pdbe.org/2ojm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2ojm RCSB], [http://www.ebi.ac.uk/pdbsum/2ojm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2ojm 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=2ojm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ojm OCA], [https://pdbe.org/2ojm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ojm RCSB], [https://www.ebi.ac.uk/pdbsum/2ojm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ojm ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/MORO_MORSA MORO_MORSA]] Exhibits broad spectrum antimicrobial activity against Gram-positive and Gram-negative bacteria as well as against a variety of fungi. Has hemolytic activity. Seems to disrupt the membranes by adopting an alpha helical conformation and forming toroidal pores.<ref>PMID:11713517</ref> <ref>PMID:17253775</ref>
+[[https://www.uniprot.org/uniprot/MORO_MORSA MORO_MORSA]] Exhibits broad spectrum antimicrobial activity against Gram-positive and Gram-negative bacteria as well as against a variety of fungi. Has hemolytic activity. Seems to disrupt the membranes by adopting an alpha helical conformation and forming toroidal pores.<ref>PMID:11713517</ref> <ref>PMID:17253775</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==

2ojm

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Revision as of 07:51, 2 March 2022

Solution structure and cell selectivity of Piscidin 1 and its analogues

Structural highlights

Function

Publication Abstract from PubMed

References

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