1hu5: Difference between revisions
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==SOLUTION STRUCTURE OF OVISPIRIN-1== | |||
<StructureSection load='1hu5' size='340' side='right'caption='[[1hu5]]' scene=''> | |||
== Structural highlights == | |||
| | <table><tr><td colspan='2'>[[1hu5]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HU5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HU5 FirstGlance]. <br> | ||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1hu5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hu5 OCA], [https://pdbe.org/1hu5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hu5 RCSB], [https://www.ebi.ac.uk/pdbsum/1hu5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hu5 ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
''' | == Publication Abstract from PubMed == | ||
== | |||
We studied three model antibacterial peptides that resembled the N-terminal 18 amino acids of SMAP-29, an alpha-helical, antimicrobial peptide of sheep. Although the parent compound, ovispirin-1 (KNLRR IIRKI IHIIK KYG), was potently antimicrobial, it was also highly cytotoxic to human epithelial cells and hemolytic for human erythrocytes. Single residue substitutions to ovispirin-1 yielded two substantially less cytotoxic peptides (novispirins), with intact antimicrobial properties. One of these, novispirin G-10, differed from ovispirin-1 only by containing glycine at position 10, instead of isoleucine. The other, novispirin T-7, contained threonine instead of isoleucine at position 7. We determined the three-dimensional solution structures of all three peptides by circular dichroism spectroscopy and two-dimensional nuclear magnetic resonance spectroscopy. Although all retained an amphipathic helical structure in 2,2,2-trifluoroethanol, they manifested subtle fine-structural changes that evidently impacted their activities greatly. These findings show that simple structural modifications can 'fine-tune' an antimicrobial peptide to minimize unwanted cytotoxicity while retaining its desired activity. | We studied three model antibacterial peptides that resembled the N-terminal 18 amino acids of SMAP-29, an alpha-helical, antimicrobial peptide of sheep. Although the parent compound, ovispirin-1 (KNLRR IIRKI IHIIK KYG), was potently antimicrobial, it was also highly cytotoxic to human epithelial cells and hemolytic for human erythrocytes. Single residue substitutions to ovispirin-1 yielded two substantially less cytotoxic peptides (novispirins), with intact antimicrobial properties. One of these, novispirin G-10, differed from ovispirin-1 only by containing glycine at position 10, instead of isoleucine. The other, novispirin T-7, contained threonine instead of isoleucine at position 7. We determined the three-dimensional solution structures of all three peptides by circular dichroism spectroscopy and two-dimensional nuclear magnetic resonance spectroscopy. Although all retained an amphipathic helical structure in 2,2,2-trifluoroethanol, they manifested subtle fine-structural changes that evidently impacted their activities greatly. These findings show that simple structural modifications can 'fine-tune' an antimicrobial peptide to minimize unwanted cytotoxicity while retaining its desired activity. | ||
Impact of single-residue mutations on the structure and function of ovispirin/novispirin antimicrobial peptides.,Sawai MV, Waring AJ, Kearney WR, McCray PB Jr, Forsyth WR, Lehrer RI, Tack BF Protein Eng. 2002 Mar;15(3):225-32. PMID:11932493<ref>PMID:11932493</ref> | |||
Impact of single-residue mutations on the structure and function of ovispirin/novispirin antimicrobial peptides., Sawai MV, Waring AJ, Kearney WR, McCray PB Jr, Forsyth WR, Lehrer RI, Tack BF | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1hu5" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Forsyth WR]] | |||
[[Category: Kearney WR]] | |||
[[Category: Lehrer RI]] | |||
[[Category: McCray Jr PB]] | |||
[[Category: Sawai MV]] | |||
[[Category: Tack BF]] | |||
[[Category: Waring AJ]] | |||
Latest revision as of 18:39, 29 November 2023
SOLUTION STRUCTURE OF OVISPIRIN-1
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