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.

5xrx

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Current revision

EFK17DA structure in Microgel MAA60

Structural highlights

5xrx is a 1 chain structure with sequence from Homo sapiens. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CAMP_HUMAN Binds to bacterial lipopolysaccharides (LPS), has antibacterial activity.^[1] ^[2]

Publication Abstract from PubMed

Successful use of microgels as delivery systems of antimicrobial peptides (AMPs) requires control of factors determining peptide loading and release to/from the microgels as well as of membrane interactions of both microgel particles and released peptides. Addressing these, we here investigate effects of microgel charge density and conformationally induced peptide amphiphilicity on AMP loading and release using detailed nuclear magnetic resonance (NMR) structural studies combined with ellipsometry, isothermal titration calorimetry, circular dichroism, and light scattering. In parallel, consequences of peptide loading and release for membrane interactions and antimicrobial effects were investigated. In doing so, poly(ethyl acrylate-co-methacrylic acid) microgels were found to incorporate the cationic AMPs EFK17a (EFKRIVQRIKDFLRNLV) and its partially d-amino acid-substituted variant EFK17da (E(dF)KR(dI)VQR(dI)KD(dF)LRNLV). Peptide incorporation was found to increase with increasing with microgel charge density and peptide amphiphilicity. After microgel incorporation, which appeared to occur preferentially in the microgel core, NMR showed EFK17a to form a helix with pronounced amphiphilicity, while EFK17da displayed a folded conformation, stabilized by a hydrophobic hub consisting of aromatic/aromatic and aliphatic/aromatic interactions, resulting in much lower amphiphilicity. Under wide ranges of peptide loading, the microgels displayed net negative z-potential. Such negatively charged microgels do not bind to, nor lyse, bacteria-mimicking membranes. Instead, membrane disruption in these systems is mediated largely by peptide release, which in turn is promoted at higher ionic strength and lower peptide amphiphilicity. Analogously, antimicrobial effects against Escherichia coli were found to be dictated by peptide release. Taken together, the findings show that peptide loading, packing, and release strongly affect the performance of microgels as AMP delivery systems, effects that can be tuned by (conformationally induced) peptide amphiphilicity and by microgel charge density.

Conformational Aspects of High Content Packing of Antimicrobial Peptides in Polymer Microgels.,Singh S, Datta A, Borro BC, Davoudi M, Schmidtchen A, Bhunia A, Malmsten M ACS Appl Mater Interfaces. 2017 Nov 22;9(46):40094-40106. doi:, 10.1021/acsami.7b13714. Epub 2017 Nov 9. PMID:29087182^[3]

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

References

↑ Li X, Li Y, Han H, Miller DW, Wang G. Solution structures of human LL-37 fragments and NMR-based identification of a minimal membrane-targeting antimicrobial and anticancer region. J Am Chem Soc. 2006 May 3;128(17):5776-85. PMID:16637646 doi:10.1021/ja0584875
↑ Wang G. Structures of human host defense cathelicidin LL-37 and its smallest antimicrobial peptide KR-12 in lipid micelles. J Biol Chem. 2008 Nov 21;283(47):32637-43. Epub 2008 Sep 25. PMID:18818205 doi:10.1074/jbc.M805533200
↑ Singh S, Datta A, Borro BC, Davoudi M, Schmidtchen A, Bhunia A, Malmsten M. Conformational Aspects of High Content Packing of Antimicrobial Peptides in Polymer Microgels. ACS Appl Mater Interfaces. 2017 Nov 22;9(46):40094-40106. doi:, 10.1021/acsami.7b13714. Epub 2017 Nov 9. PMID:29087182 doi:http://dx.doi.org/10.1021/acsami.7b13714

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/5xrx"

Categories: Homo sapiens | Large Structures | Bhunia A | Datta A

@@ Line 1: / Line 1: @@
 ==EFK17DA structure in Microgel MAA60==
-<StructureSection load='5xrx' size='340' side='right'caption='[[5xrx]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
+<StructureSection load='5xrx' size='340' side='right'caption='[[5xrx]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5xrx]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XRX OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5XRX FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5xrx]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XRX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5XRX FirstGlance]. <br>
-</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=5xrx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xrx OCA], [http://pdbe.org/5xrx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5xrx RCSB], [http://www.ebi.ac.uk/pdbsum/5xrx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5xrx ProSAT]</span></td></tr>
+</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=5xrx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xrx OCA], [https://pdbe.org/5xrx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5xrx RCSB], [https://www.ebi.ac.uk/pdbsum/5xrx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5xrx ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/CAMP_HUMAN CAMP_HUMAN]] Binds to bacterial lipopolysaccharides (LPS), has antibacterial activity.<ref>PMID:16637646</ref> <ref>PMID:18818205</ref>
+[https://www.uniprot.org/uniprot/CAMP_HUMAN CAMP_HUMAN] Binds to bacterial lipopolysaccharides (LPS), has antibacterial activity.<ref>PMID:16637646</ref> <ref>PMID:18818205</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 21: / Line 21: @@
 __TOC__
 </StructureSection>
+[[Category: Homo sapiens]]
 [[Category: Large Structures]]
-[[Category: Bhunia, A]]
+[[Category: Bhunia A]]
-[[Category: Datta, A]]
+[[Category: Datta A]]
-[[Category: Antimicrobial peptide]]
-[[Category: Antimicrobial protein]]
-[[Category: D amino acid isomer]]
-[[Category: Helical and coiled structure]]
-[[Category: Peptide derived from human ll37]]

5xrx

From Proteopedia

Current revision

EFK17DA structure in Microgel MAA60

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox