1hu5
From Proteopedia
(New page: 200px<br /><applet load="1hu5" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hu5" /> '''SOLUTION STRUCTURE OF OVISPIRIN-1'''<br /> ...) |
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| - | [[Image:1hu5.gif|left|200px]]<br /><applet load="1hu5" size=" | + | [[Image:1hu5.gif|left|200px]]<br /><applet load="1hu5" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1hu5" /> | caption="1hu5" /> | ||
'''SOLUTION STRUCTURE OF OVISPIRIN-1'''<br /> | '''SOLUTION STRUCTURE OF OVISPIRIN-1'''<br /> | ||
==Overview== | ==Overview== | ||
| - | We studied three model antibacterial peptides that resembled the | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 1HU5 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http:// | + | 1HU5 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HU5 OCA]. |
==Reference== | ==Reference== | ||
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11932493 11932493] | 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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11932493 11932493] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
| - | [[Category: Forsyth, W | + | [[Category: Forsyth, W R.]] |
| - | [[Category: Jr., P | + | [[Category: Jr., P B.McCray.]] |
| - | [[Category: Kearney, W | + | [[Category: Kearney, W R.]] |
| - | [[Category: Lehrer, R | + | [[Category: Lehrer, R I.]] |
| - | [[Category: Sawai, M | + | [[Category: Sawai, M V.]] |
| - | [[Category: Tack, B | + | [[Category: Tack, B F.]] |
| - | [[Category: Waring, A | + | [[Category: Waring, A J.]] |
[[Category: peptide]] | [[Category: peptide]] | ||
[[Category: solution structure]] | [[Category: solution structure]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:04:50 2008'' |
Revision as of 11:04, 21 February 2008
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SOLUTION STRUCTURE OF OVISPIRIN-1
Overview
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.
About this Structure
1HU5 is a Protein complex structure of sequences from [1]. Full crystallographic information is available from OCA.
Reference
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
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