Mechanism of antibacterial action of a synthetic peptide with an Ala-peptoid residue based on the scorpion-derived antimicrobial peptide IsCT
A novel bacterial cell-selective antimicrobial peptide, IsCT-P (ILKKIWKPIKKLF-NH₂), was designed based on the scorpion-derived α-helical antimicrobial peptide, IsCT. Here, we investigated the effect of substituting Pro⁸ of IsCT-P with the Ala-peptoid residue (N-methylglycine) on the peptide's s...
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| Veröffentlicht in: | Biotechnology letters 2006-09, Vol.28 (18), p.1431-1437 |
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| creator | Lim, Shin Saeng Yoon, Sang-Pil Park, Yoonkyoung Zhu, Wan Long Park, Il-Seon Hahm, Kyung -Soo Shin, Song Yub |
| description | A novel bacterial cell-selective antimicrobial peptide, IsCT-P (ILKKIWKPIKKLF-NH₂), was designed based on the scorpion-derived α-helical antimicrobial peptide, IsCT. Here, we investigated the effect of substituting Pro⁸ of IsCT-P with the Ala-peptoid residue (N-methylglycine) on the peptide's structure and mechanism of action. Circular dichroism analysis revealed that the modified peptide, IsCT-a, has a much lower α-helicity than IsCT-P in membrane mimicking conditions, suggesting the peptoid residue provides much more structural flexibility than the proline residue. IsCT-a was also much less effective than IsCT-P at causing leakage of fluorescent dye entrapped within negatively charged vesicles and at dissipating the membrane potential of Staphylococcus aureus. Collectively, our results suggest that the antibacterial action of IsCT-a is due to the inhibition of intracellular targets rather than the disruption and depolarization of bacterial cell membranes. |
| doi_str_mv | 10.1007/s10529-006-9107-6 |
| format | Article |
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Here, we investigated the effect of substituting Pro⁸ of IsCT-P with the Ala-peptoid residue (N-methylglycine) on the peptide's structure and mechanism of action. Circular dichroism analysis revealed that the modified peptide, IsCT-a, has a much lower α-helicity than IsCT-P in membrane mimicking conditions, suggesting the peptoid residue provides much more structural flexibility than the proline residue. IsCT-a was also much less effective than IsCT-P at causing leakage of fluorescent dye entrapped within negatively charged vesicles and at dissipating the membrane potential of Staphylococcus aureus. Collectively, our results suggest that the antibacterial action of IsCT-a is due to the inhibition of intracellular targets rather than the disruption and depolarization of bacterial cell membranes.</description><identifier>ISSN: 0141-5492</identifier><identifier>EISSN: 1573-6776</identifier><identifier>DOI: 10.1007/s10529-006-9107-6</identifier><identifier>PMID: 16871429</identifier><identifier>CODEN: BILED3</identifier><language>eng</language><publisher>Dordrecht: Dordrecht : Kluwer Academic Publishers</publisher><subject>Ala-peptoid residue ; Amino Acid Sequence ; Anti-Infective Agents - pharmacology ; Antibacterial action ; Antimicrobial Cationic Peptides - chemistry ; Antimicrobial Cationic Peptides - pharmacology ; Bacteria ; Biological and medical sciences ; Biotechnology ; Cell Membrane - drug effects ; Circular Dichroism ; Fluoresceins - metabolism ; Fundamental and applied biological sciences. Psychology ; Hemolytic Agents - pharmacology ; Humans ; Liposomes - metabolism ; Mechanism ; Membrane Potentials - drug effects ; Microbiology ; Peptides ; Peptoids - pharmacology ; Residues ; Scorpion Venoms - chemistry ; Scorpion-derived antimicrobial peptide IsCT ; Staphylococcus aureus ; Staphylococcus infections ; Structuralflexibility</subject><ispartof>Biotechnology letters, 2006-09, Vol.28 (18), p.1431-1437</ispartof><rights>2006 INIST-CNRS</rights><rights>Springer Science+Business Media, Inc. 2006</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c443t-3bb5f670cf8af0eb8e0dec3fadce4e8e7313b336a32aa545beeeaa2f62a6d5213</citedby><cites>FETCH-LOGICAL-c443t-3bb5f670cf8af0eb8e0dec3fadce4e8e7313b336a32aa545beeeaa2f62a6d5213</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27901,27902</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=18129723$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/16871429$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Lim, Shin Saeng</creatorcontrib><creatorcontrib>Yoon, Sang-Pil</creatorcontrib><creatorcontrib>Park, Yoonkyoung</creatorcontrib><creatorcontrib>Zhu, Wan Long</creatorcontrib><creatorcontrib>Park, Il-Seon</creatorcontrib><creatorcontrib>Hahm, Kyung -Soo</creatorcontrib><creatorcontrib>Shin, Song Yub</creatorcontrib><title>Mechanism of antibacterial action of a synthetic peptide with an Ala-peptoid residue based on the scorpion-derived antimicrobial peptide IsCT</title><title>Biotechnology letters</title><addtitle>Biotechnol Lett</addtitle><description>A novel bacterial cell-selective antimicrobial peptide, IsCT-P (ILKKIWKPIKKLF-NH₂), was designed based on the scorpion-derived α-helical antimicrobial peptide, IsCT. Here, we investigated the effect of substituting Pro⁸ of IsCT-P with the Ala-peptoid residue (N-methylglycine) on the peptide's structure and mechanism of action. Circular dichroism analysis revealed that the modified peptide, IsCT-a, has a much lower α-helicity than IsCT-P in membrane mimicking conditions, suggesting the peptoid residue provides much more structural flexibility than the proline residue. IsCT-a was also much less effective than IsCT-P at causing leakage of fluorescent dye entrapped within negatively charged vesicles and at dissipating the membrane potential of Staphylococcus aureus. Collectively, our results suggest that the antibacterial action of IsCT-a is due to the inhibition of intracellular targets rather than the disruption and depolarization of bacterial cell membranes.</description><subject>Ala-peptoid residue</subject><subject>Amino Acid Sequence</subject><subject>Anti-Infective Agents - pharmacology</subject><subject>Antibacterial action</subject><subject>Antimicrobial Cationic Peptides - chemistry</subject><subject>Antimicrobial Cationic Peptides - pharmacology</subject><subject>Bacteria</subject><subject>Biological and medical sciences</subject><subject>Biotechnology</subject><subject>Cell Membrane - drug effects</subject><subject>Circular Dichroism</subject><subject>Fluoresceins - metabolism</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Hemolytic Agents - pharmacology</subject><subject>Humans</subject><subject>Liposomes - metabolism</subject><subject>Mechanism</subject><subject>Membrane Potentials - drug effects</subject><subject>Microbiology</subject><subject>Peptides</subject><subject>Peptoids - pharmacology</subject><subject>Residues</subject><subject>Scorpion Venoms - chemistry</subject><subject>Scorpion-derived antimicrobial peptide IsCT</subject><subject>Staphylococcus aureus</subject><subject>Staphylococcus infections</subject><subject>Structuralflexibility</subject><issn>0141-5492</issn><issn>1573-6776</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2006</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>BENPR</sourceid><recordid>eNp9kc1uFDEQhC0EIpvAA3ABCwk4GfzvmWO0IhApiAPJ2erx9LCO5mexZ4LyELwzHnZRJA6cbLW-qupWEfJC8PeCc_chC25kzTi3rBbcMfuIbIRxilnn7GOy4UILZnQtT8hpzrec89px95ScCFs5oWW9Ib--YNjBGPNAp47COMcGwowpQk_LJ07jnznN9-O8wzkGusf9HFukP-O8KwJ63gNbZ1NsacIc2wVpAxlbWrRFQ3OY0r4YsbbY3pX5mjLEkKZmTfnrd5m318_Ikw76jM-P7xm5ufh4vf3Mrr5-utyeX7GgtZqZahrTWcdDV0HHsamQtxhUB21AjRU6JVSjlAUlAYw2DSICyM5KsK2RQp2RdwfffZp-LJhnP8QcsO9hxGnJ3mklXSUqU8i3_yVFXTtttCrg63_A22lJY7nCO6VdXTm95ooDVI7POWHn9ykOkO694H6t1B8q9aVSv1bqbdG8PBovzYDtg-LYYQHeHAHIAfouwRhifuAqIWsn1w1fHbgOJg_fU2FuvkkuFBdCGO2M-g1KXbTn</recordid><startdate>20060901</startdate><enddate>20060901</enddate><creator>Lim, Shin Saeng</creator><creator>Yoon, Sang-Pil</creator><creator>Park, Yoonkyoung</creator><creator>Zhu, Wan Long</creator><creator>Park, Il-Seon</creator><creator>Hahm, Kyung -Soo</creator><creator>Shin, Song Yub</creator><general>Dordrecht : Kluwer Academic Publishers</general><general>Springer</general><general>Springer Nature B.V</general><scope>FBQ</scope><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>3V.</scope><scope>7QL</scope><scope>7QR</scope><scope>7T7</scope><scope>7TB</scope><scope>7U5</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>88I</scope><scope>8AO</scope><scope>8FD</scope><scope>8FE</scope><scope>8FG</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABJCF</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BGLVJ</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>L6V</scope><scope>L7M</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M2P</scope><scope>M7N</scope><scope>M7P</scope><scope>M7S</scope><scope>P64</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PTHSS</scope><scope>Q9U</scope><scope>7QO</scope></search><sort><creationdate>20060901</creationdate><title>Mechanism of antibacterial action of a synthetic peptide with an Ala-peptoid residue based on the scorpion-derived antimicrobial peptide IsCT</title><author>Lim, Shin Saeng ; Yoon, Sang-Pil ; Park, Yoonkyoung ; Zhu, Wan Long ; Park, Il-Seon ; Hahm, Kyung -Soo ; Shin, Song Yub</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c443t-3bb5f670cf8af0eb8e0dec3fadce4e8e7313b336a32aa545beeeaa2f62a6d5213</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2006</creationdate><topic>Ala-peptoid residue</topic><topic>Amino Acid Sequence</topic><topic>Anti-Infective Agents - pharmacology</topic><topic>Antibacterial action</topic><topic>Antimicrobial Cationic Peptides - chemistry</topic><topic>Antimicrobial Cationic Peptides - pharmacology</topic><topic>Bacteria</topic><topic>Biological and medical sciences</topic><topic>Biotechnology</topic><topic>Cell Membrane - drug effects</topic><topic>Circular Dichroism</topic><topic>Fluoresceins - metabolism</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Hemolytic Agents - pharmacology</topic><topic>Humans</topic><topic>Liposomes - metabolism</topic><topic>Mechanism</topic><topic>Membrane Potentials - drug effects</topic><topic>Microbiology</topic><topic>Peptides</topic><topic>Peptoids - pharmacology</topic><topic>Residues</topic><topic>Scorpion Venoms - chemistry</topic><topic>Scorpion-derived antimicrobial peptide IsCT</topic><topic>Staphylococcus aureus</topic><topic>Staphylococcus infections</topic><topic>Structuralflexibility</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Lim, Shin Saeng</creatorcontrib><creatorcontrib>Yoon, Sang-Pil</creatorcontrib><creatorcontrib>Park, Yoonkyoung</creatorcontrib><creatorcontrib>Zhu, Wan Long</creatorcontrib><creatorcontrib>Park, Il-Seon</creatorcontrib><creatorcontrib>Hahm, Kyung -Soo</creatorcontrib><creatorcontrib>Shin, Song 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letters</jtitle><addtitle>Biotechnol Lett</addtitle><date>2006-09-01</date><risdate>2006</risdate><volume>28</volume><issue>18</issue><spage>1431</spage><epage>1437</epage><pages>1431-1437</pages><issn>0141-5492</issn><eissn>1573-6776</eissn><coden>BILED3</coden><abstract>A novel bacterial cell-selective antimicrobial peptide, IsCT-P (ILKKIWKPIKKLF-NH₂), was designed based on the scorpion-derived α-helical antimicrobial peptide, IsCT. Here, we investigated the effect of substituting Pro⁸ of IsCT-P with the Ala-peptoid residue (N-methylglycine) on the peptide's structure and mechanism of action. Circular dichroism analysis revealed that the modified peptide, IsCT-a, has a much lower α-helicity than IsCT-P in membrane mimicking conditions, suggesting the peptoid residue provides much more structural flexibility than the proline residue. IsCT-a was also much less effective than IsCT-P at causing leakage of fluorescent dye entrapped within negatively charged vesicles and at dissipating the membrane potential of Staphylococcus aureus. Collectively, our results suggest that the antibacterial action of IsCT-a is due to the inhibition of intracellular targets rather than the disruption and depolarization of bacterial cell membranes.</abstract><cop>Dordrecht</cop><pub>Dordrecht : Kluwer Academic Publishers</pub><pmid>16871429</pmid><doi>10.1007/s10529-006-9107-6</doi><tpages>7</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0141-5492 |
| ispartof | Biotechnology letters, 2006-09, Vol.28 (18), p.1431-1437 |
| issn | 0141-5492 1573-6776 |
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| source | MEDLINE; Springer Nature - Complete Springer Journals |
| subjects | Ala-peptoid residue Amino Acid Sequence Anti-Infective Agents - pharmacology Antibacterial action Antimicrobial Cationic Peptides - chemistry Antimicrobial Cationic Peptides - pharmacology Bacteria Biological and medical sciences Biotechnology Cell Membrane - drug effects Circular Dichroism Fluoresceins - metabolism Fundamental and applied biological sciences. Psychology Hemolytic Agents - pharmacology Humans Liposomes - metabolism Mechanism Membrane Potentials - drug effects Microbiology Peptides Peptoids - pharmacology Residues Scorpion Venoms - chemistry Scorpion-derived antimicrobial peptide IsCT Staphylococcus aureus Staphylococcus infections Structuralflexibility |
| title | Mechanism of antibacterial action of a synthetic peptide with an Ala-peptoid residue based on the scorpion-derived antimicrobial peptide IsCT |
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