1hr1
From Proteopedia
(New page: 200px<br /><applet load="1hr1" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hr1" /> '''STRUCTURE OF AN INDOLICIDIN PEPTIDE DERIVATI...) |
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| - | [[Image:1hr1.jpg|left|200px]]<br /><applet load="1hr1" size=" | + | [[Image:1hr1.jpg|left|200px]]<br /><applet load="1hr1" size="350" color="white" frame="true" align="right" spinBox="true" |
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'''STRUCTURE OF AN INDOLICIDIN PEPTIDE DERIVATIVE WITH P-->A SUBSTITUTION'''<br /> | '''STRUCTURE OF AN INDOLICIDIN PEPTIDE DERIVATIVE WITH P-->A SUBSTITUTION'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Indolicidin, an antimicrobial peptide with a unique amino acid sequence | + | Indolicidin, an antimicrobial peptide with a unique amino acid sequence (ILPWKWPWWPWRR-NH(2)) is found in bovine neutrophils. A derivative of indolicidin, CP10A, has alanine residues substituted for proline residues and has improved activity against Gram-positive organisms. Transmission electron microscopy of Staphylococcus aureus and Staphylococcus epidermidis treated with CP10A showed mesosome-like structures in the cytoplasm. The peptide at 2-fold the minimal inhibitory concentration did not show significant killing of S. aureus ISP67 (a histidine, uridine, and thymidine auxotroph) but did show an early effect on histidine and uridine incorporation and, later, an effect on thymidine incorporation. Upon interaction with liposomes, detergents, and lipoteichoic acid, CP10A was shown by circular dichroism spectroscopy to undergo a change in secondary structure. Fluorescence spectroscopy indicated that the tryptophan residues were located at the hydrophobic/hydrophilic interface of liposomes and detergent micelles and were inaccessible to the aqueous quencher KI. The three-dimensional structure of CP10A in the lipid mimetic dodecylphosphocholine was determined using two-dimensional NMR methods and was characterized as a short, amphipathic helical structure, whereas indolicidin was previously shown to have an extended structure. These studies have introduced a cationic peptide with a unique structure and an ability to interact with membranes and to affect intracellular synthesis of proteins, RNA, and DNA. |
==About this Structure== | ==About this Structure== | ||
| - | 1HR1 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ] with NH2 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1HR1 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ] with <scene name='pdbligand=NH2:'>NH2</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HR1 OCA]. |
==Reference== | ==Reference== | ||
Structure and mechanism of action of an indolicidin peptide derivative with improved activity against gram-positive bacteria., Friedrich CL, Rozek A, Patrzykat A, Hancock RE, J Biol Chem. 2001 Jun 29;276(26):24015-22. Epub 2001 Apr 9. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11294848 11294848] | Structure and mechanism of action of an indolicidin peptide derivative with improved activity against gram-positive bacteria., Friedrich CL, Rozek A, Patrzykat A, Hancock RE, J Biol Chem. 2001 Jun 29;276(26):24015-22. Epub 2001 Apr 9. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11294848 11294848] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Friedrich, C | + | [[Category: Friedrich, C L.]] |
| - | [[Category: Hancock, R | + | [[Category: Hancock, R E.W.]] |
[[Category: Patrzykat, A.]] | [[Category: Patrzykat, A.]] | ||
[[Category: Rozek, A.]] | [[Category: Rozek, A.]] | ||
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[[Category: cationic antimicrobial peptide]] | [[Category: cationic antimicrobial peptide]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:04:00 2008'' |
Revision as of 11:04, 21 February 2008
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STRUCTURE OF AN INDOLICIDIN PEPTIDE DERIVATIVE WITH P-->A SUBSTITUTION
Overview
Indolicidin, an antimicrobial peptide with a unique amino acid sequence (ILPWKWPWWPWRR-NH(2)) is found in bovine neutrophils. A derivative of indolicidin, CP10A, has alanine residues substituted for proline residues and has improved activity against Gram-positive organisms. Transmission electron microscopy of Staphylococcus aureus and Staphylococcus epidermidis treated with CP10A showed mesosome-like structures in the cytoplasm. The peptide at 2-fold the minimal inhibitory concentration did not show significant killing of S. aureus ISP67 (a histidine, uridine, and thymidine auxotroph) but did show an early effect on histidine and uridine incorporation and, later, an effect on thymidine incorporation. Upon interaction with liposomes, detergents, and lipoteichoic acid, CP10A was shown by circular dichroism spectroscopy to undergo a change in secondary structure. Fluorescence spectroscopy indicated that the tryptophan residues were located at the hydrophobic/hydrophilic interface of liposomes and detergent micelles and were inaccessible to the aqueous quencher KI. The three-dimensional structure of CP10A in the lipid mimetic dodecylphosphocholine was determined using two-dimensional NMR methods and was characterized as a short, amphipathic helical structure, whereas indolicidin was previously shown to have an extended structure. These studies have introduced a cationic peptide with a unique structure and an ability to interact with membranes and to affect intracellular synthesis of proteins, RNA, and DNA.
About this Structure
1HR1 is a Single protein structure of sequence from [1] with as ligand. Full crystallographic information is available from OCA.
Reference
Structure and mechanism of action of an indolicidin peptide derivative with improved activity against gram-positive bacteria., Friedrich CL, Rozek A, Patrzykat A, Hancock RE, J Biol Chem. 2001 Jun 29;276(26):24015-22. Epub 2001 Apr 9. PMID:11294848
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