Development of novel antibacterial peptides that kill resistant isolates
The rapid emergence of bacterial strains that are resistant to current antibiotics requires the development of novel types of antimicrobial compounds. Proline-rich cationic antibacterial peptides such as pyrrhocoricin kill responsive bacteria by binding to the 70 kDa heat shock protein DnaK and inhi...
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| Veröffentlicht in: | Peptides (New York, N.Y. : 1980) N.Y. : 1980), 2002-12, Vol.23 (12), p.2071-2083 |
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| container_title | Peptides (New York, N.Y. : 1980) |
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| creator | Cudic, Mare Condie, Barry A. Weiner, Daniel J. Lysenko, Elena S. Xiang, Zhi Q. Insug, O. Bulet, Philippe Otvos, Laszlo |
| description | The rapid emergence of bacterial strains that are resistant to current antibiotics requires the development of novel types of antimicrobial compounds. Proline-rich cationic antibacterial peptides such as pyrrhocoricin kill responsive bacteria by binding to the 70
kDa heat shock protein DnaK and inhibiting protein folding. We designed and synthesized multiply protected dimeric analogs of pyrrhocoricin and optimized the in vitro antibacterial efficacy assays for peptide antibiotics. Pyrrhocoricin and the designed dimers killed β-lactam, tetracycline- or aminoglycoside-resistant strains of
Escherichia coli,
Salmonella typhimurium,
Klebsiella pneumoniae,
Haemophilus influenzae, and
Moraxella catarrhalis in the submicromolar or low micromolar concentration range. One of the peptides also killed
Pseudomonas aeruginosa. The designed dimers showed improved stability in mammalian sera compared to the native analog. In a murine
H. influenzae lung infection model, a single dose of a dimeric pyrrhocoricin analog reduced the bacteria in the bronchoalveolar lavage when delivered intranasally. The solid-phase synthesis was optimized for large-scale laboratory preparations. |
| doi_str_mv | 10.1016/S0196-9781(02)00244-9 |
| format | Article |
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kDa heat shock protein DnaK and inhibiting protein folding. We designed and synthesized multiply protected dimeric analogs of pyrrhocoricin and optimized the in vitro antibacterial efficacy assays for peptide antibiotics. Pyrrhocoricin and the designed dimers killed β-lactam, tetracycline- or aminoglycoside-resistant strains of
Escherichia coli,
Salmonella typhimurium,
Klebsiella pneumoniae,
Haemophilus influenzae, and
Moraxella catarrhalis in the submicromolar or low micromolar concentration range. One of the peptides also killed
Pseudomonas aeruginosa. The designed dimers showed improved stability in mammalian sera compared to the native analog. In a murine
H. influenzae lung infection model, a single dose of a dimeric pyrrhocoricin analog reduced the bacteria in the bronchoalveolar lavage when delivered intranasally. The solid-phase synthesis was optimized for large-scale laboratory preparations.</description><identifier>ISSN: 0196-9781</identifier><identifier>EISSN: 1873-5169</identifier><identifier>DOI: 10.1016/S0196-9781(02)00244-9</identifier><identifier>PMID: 12535685</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Anti-Bacterial Agents - pharmacology ; Antimicrobial Cationic Peptides - pharmacology ; Antimicrobial peptides ; Bacteria - drug effects ; Bacteriocidal analogs ; Drug Resistance, Bacterial - physiology ; Haemophilus influenzae - drug effects ; In vivo protection ; Insect Proteins ; Life Sciences ; Methylation ; Peptides - pharmacology ; Proline-rich ; Pseudomonas aeruginosa - drug effects ; Serum stability ; Solid-phase synthesis</subject><ispartof>Peptides (New York, N.Y. : 1980), 2002-12, Vol.23 (12), p.2071-2083</ispartof><rights>2002 Elsevier Science Inc.</rights><rights>Distributed under a Creative Commons Attribution 4.0 International License</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c426t-9ef1fb52ba23c99a1e566248fdf653eaf3ad46c418ffb9af6857edbba892f1143</citedby><cites>FETCH-LOGICAL-c426t-9ef1fb52ba23c99a1e566248fdf653eaf3ad46c418ffb9af6857edbba892f1143</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0196978102002449$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>230,314,776,780,881,3537,27901,27902,65306</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/12535685$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://hal.science/hal-03828709$$DView record in HAL$$Hfree_for_read</backlink></links><search><creatorcontrib>Cudic, Mare</creatorcontrib><creatorcontrib>Condie, Barry A.</creatorcontrib><creatorcontrib>Weiner, Daniel J.</creatorcontrib><creatorcontrib>Lysenko, Elena S.</creatorcontrib><creatorcontrib>Xiang, Zhi Q.</creatorcontrib><creatorcontrib>Insug, O.</creatorcontrib><creatorcontrib>Bulet, Philippe</creatorcontrib><creatorcontrib>Otvos, Laszlo</creatorcontrib><title>Development of novel antibacterial peptides that kill resistant isolates</title><title>Peptides (New York, N.Y. : 1980)</title><addtitle>Peptides</addtitle><description>The rapid emergence of bacterial strains that are resistant to current antibiotics requires the development of novel types of antimicrobial compounds. Proline-rich cationic antibacterial peptides such as pyrrhocoricin kill responsive bacteria by binding to the 70
kDa heat shock protein DnaK and inhibiting protein folding. We designed and synthesized multiply protected dimeric analogs of pyrrhocoricin and optimized the in vitro antibacterial efficacy assays for peptide antibiotics. Pyrrhocoricin and the designed dimers killed β-lactam, tetracycline- or aminoglycoside-resistant strains of
Escherichia coli,
Salmonella typhimurium,
Klebsiella pneumoniae,
Haemophilus influenzae, and
Moraxella catarrhalis in the submicromolar or low micromolar concentration range. One of the peptides also killed
Pseudomonas aeruginosa. The designed dimers showed improved stability in mammalian sera compared to the native analog. In a murine
H. influenzae lung infection model, a single dose of a dimeric pyrrhocoricin analog reduced the bacteria in the bronchoalveolar lavage when delivered intranasally. The solid-phase synthesis was optimized for large-scale laboratory preparations.</description><subject>Anti-Bacterial Agents - pharmacology</subject><subject>Antimicrobial Cationic Peptides - pharmacology</subject><subject>Antimicrobial peptides</subject><subject>Bacteria - drug effects</subject><subject>Bacteriocidal analogs</subject><subject>Drug Resistance, Bacterial - physiology</subject><subject>Haemophilus influenzae - drug effects</subject><subject>In vivo protection</subject><subject>Insect Proteins</subject><subject>Life Sciences</subject><subject>Methylation</subject><subject>Peptides - pharmacology</subject><subject>Proline-rich</subject><subject>Pseudomonas aeruginosa - drug effects</subject><subject>Serum stability</subject><subject>Solid-phase synthesis</subject><issn>0196-9781</issn><issn>1873-5169</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2002</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkU9vEzEQxS0EoiHwEUB7QvSw4P9rn1BVKEGKxAE4W17vWDU468V2IvXb4zRRe-xpNKPfzDy9h9Bbgj8STOSnn5ho2etBkQ-YXmJMOe_1M7QiamC9IFI_R6sH5AK9KuUPxphzrV6iC0IFE1KJFdp8gQPEtOxgrl3y3Zxa29m5htG6CjnY2C2w1DBB6eqtrd3fEGOXoYRSG9aFkqKtUF6jF97GAm_OdY1-33z9db3ptz--fb--2vaOU1l7DZ74UdDRUua0tgSElJQrP3kpGFjP7MSl40R5P2rrm8gBpnG0SlNPCGdrdHm6e2ujWXLY2Xxnkg1mc7U1xxlmiqoB6wNp7PsTu-T0bw-lml0oDmK0M6R9MQNVjJFBPAk2UzHFzdk1EifQ5VRKBv8ggWBzzMXc52KOphtMzX0uRre9d-cH-3EH0-PWOYgGfD4B0Lw7BMimuACzgylkcNVMKTzx4j99YZ1G</recordid><startdate>20021201</startdate><enddate>20021201</enddate><creator>Cudic, Mare</creator><creator>Condie, Barry A.</creator><creator>Weiner, Daniel J.</creator><creator>Lysenko, Elena S.</creator><creator>Xiang, Zhi Q.</creator><creator>Insug, O.</creator><creator>Bulet, Philippe</creator><creator>Otvos, Laszlo</creator><general>Elsevier Inc</general><general>Elsevier</general><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>7T7</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>P64</scope><scope>7X8</scope><scope>1XC</scope></search><sort><creationdate>20021201</creationdate><title>Development of novel antibacterial peptides that kill resistant isolates</title><author>Cudic, Mare ; 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Proline-rich cationic antibacterial peptides such as pyrrhocoricin kill responsive bacteria by binding to the 70
kDa heat shock protein DnaK and inhibiting protein folding. We designed and synthesized multiply protected dimeric analogs of pyrrhocoricin and optimized the in vitro antibacterial efficacy assays for peptide antibiotics. Pyrrhocoricin and the designed dimers killed β-lactam, tetracycline- or aminoglycoside-resistant strains of
Escherichia coli,
Salmonella typhimurium,
Klebsiella pneumoniae,
Haemophilus influenzae, and
Moraxella catarrhalis in the submicromolar or low micromolar concentration range. One of the peptides also killed
Pseudomonas aeruginosa. The designed dimers showed improved stability in mammalian sera compared to the native analog. In a murine
H. influenzae lung infection model, a single dose of a dimeric pyrrhocoricin analog reduced the bacteria in the bronchoalveolar lavage when delivered intranasally. The solid-phase synthesis was optimized for large-scale laboratory preparations.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>12535685</pmid><doi>10.1016/S0196-9781(02)00244-9</doi><tpages>13</tpages></addata></record> |
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| ispartof | Peptides (New York, N.Y. : 1980), 2002-12, Vol.23 (12), p.2071-2083 |
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| source | MEDLINE; Elsevier ScienceDirect Journals |
| subjects | Anti-Bacterial Agents - pharmacology Antimicrobial Cationic Peptides - pharmacology Antimicrobial peptides Bacteria - drug effects Bacteriocidal analogs Drug Resistance, Bacterial - physiology Haemophilus influenzae - drug effects In vivo protection Insect Proteins Life Sciences Methylation Peptides - pharmacology Proline-rich Pseudomonas aeruginosa - drug effects Serum stability Solid-phase synthesis |
| title | Development of novel antibacterial peptides that kill resistant isolates |
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