Ontology type: schema:ScholarlyArticle
2013-02
AUTHORSLirong Li, YongHui Shi, Maureen Jepkorir Cheserek, GuanFang Su, GuoWei Le
ABSTRACTA number of research have proven that antimicrobial peptides are of greatest potential as a new class of antibiotics. Antimicrobial peptides and cell-penetrating peptides share some similar structure characteristics. In our study, a new peptide analog, APP (GLARALTRLLRQLTRQLTRA) from the cell-penetrating peptide ppTG20 (GLFRALLRLLRSLWRLLLRA), was identified simultaneously with the antibacterial mechanism of APP against Salmonella typhimurium and Streptococcus pyogenes. APP displayed potent antibacterial activity against Gram-negative and Gram-positive strains. The minimum inhibitory concentration was in the range of 2 to 4 μM. APP displayed higher cell selectivity (about 42-fold increase) as compared to the parent peptide for it decreased hemolytic activity and increased antimicrobial activity. The calcein leakage from egg yolk L-α-phosphatidylcholine (EYPC)/egg yolk L-α-phosphatidyl-DL-glycerol and EYPC/cholesterol vesicles demonstrated that APP exhibited high selectivity. The antibacterial mechanism analysis indicated that APP induced membrane permeabilization in a kinetic manner for membrane lesions allowing O-nitrophenyl-β-D-galactoside uptake into cells and potassium release from APP-treated cells. Flow cytometry analysis demonstrated that APP induced bacterial live cell membrane damage. Circular dichroism, fluorescence spectra, and gel retardation analysis confirmed that APP interacted with DNA and intercalated into the DNA base pairs after penetrating the cell membrane. Cell cycle assay showed that APP affected DNA synthesis in the cell. Our results suggested that peptides derived from the cell-penetrating peptide have the potential for antimicrobial agent development, and APP exerts its antibacterial activity by damaging bacterial cell membranes and binding to bacterial DNA to inhibit cellular functions, ultimately leading to cell death. More... »
PAGES1711-1723
http://scigraph.springernature.com/pub.10.1007/s00253-012-4352-1
DOIhttp://dx.doi.org/10.1007/s00253-012-4352-1
DIMENSIONShttps://app.dimensions.ai/details/publication/pub.1030307813
PUBMEDhttps://www.ncbi.nlm.nih.gov/pubmed/22923068
JSON-LD is the canonical representation for SciGraph data.
TIP: You can open this SciGraph record using an external JSON-LD service: JSON-LD Playground Google SDTT
[
{
"@context": "https://springernature.github.io/scigraph/jsonld/sgcontext.json",
"about": [
{
"id": "http://purl.org/au-research/vocabulary/anzsrc-for/2008/0601",
"inDefinedTermSet": "http://purl.org/au-research/vocabulary/anzsrc-for/2008/",
"name": "Biochemistry and Cell Biology",
"type": "DefinedTerm"
},
{
"id": "http://purl.org/au-research/vocabulary/anzsrc-for/2008/06",
"inDefinedTermSet": "http://purl.org/au-research/vocabulary/anzsrc-for/2008/",
"name": "Biological Sciences",
"type": "DefinedTerm"
},
{
"inDefinedTermSet": "https://www.nlm.nih.gov/mesh/",
"name": "Amino Acid Sequence",
"type": "DefinedTerm"
},
{
"inDefinedTermSet": "https://www.nlm.nih.gov/mesh/",
"name": "Anti-Bacterial Agents",
"type": "DefinedTerm"
},
{
"inDefinedTermSet": "https://www.nlm.nih.gov/mesh/",
"name": "Cell Membrane Permeability",
"type": "DefinedTerm"
},
{
"inDefinedTermSet": "https://www.nlm.nih.gov/mesh/",
"name": "Cell-Penetrating Peptides",
"type": "DefinedTerm"
},
{
"inDefinedTermSet": "https://www.nlm.nih.gov/mesh/",
"name": "Molecular Sequence Data",
"type": "DefinedTerm"
},
{
"inDefinedTermSet": "https://www.nlm.nih.gov/mesh/",
"name": "Peptides",
"type": "DefinedTerm"
},
{
"inDefinedTermSet": "https://www.nlm.nih.gov/mesh/",
"name": "Salmonella typhimurium",
"type": "DefinedTerm"
},
{
"inDefinedTermSet": "https://www.nlm.nih.gov/mesh/",
"name": "Streptococcus pyogenes",
"type": "DefinedTerm"
}
],
"author": [
{
"affiliation": {
"alternateName": "Jiangnan University",
"id": "https://www.grid.ac/institutes/grid.258151.a",
"name": [
"The State Key Laboratory of Food Science and Technology, Jiangnan University, 214122, Wuxi, Jiangsu Province, China",
"Institute of Food Nutrition and Safety, School of Food Science and Technology, Jiangnan University, 214122, Wuxi, Jiangsu Province, China"
],
"type": "Organization"
},
"familyName": "Li",
"givenName": "Lirong",
"id": "sg:person.01313346030.17",
"sameAs": [
"https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.01313346030.17"
],
"type": "Person"
},
{
"affiliation": {
"alternateName": "Jiangnan University",
"id": "https://www.grid.ac/institutes/grid.258151.a",
"name": [
"The State Key Laboratory of Food Science and Technology, Jiangnan University, 214122, Wuxi, Jiangsu Province, China",
"Institute of Food Nutrition and Safety, School of Food Science and Technology, Jiangnan University, 214122, Wuxi, Jiangsu Province, China"
],
"type": "Organization"
},
"familyName": "Shi",
"givenName": "YongHui",
"id": "sg:person.0674200354.07",
"sameAs": [
"https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.0674200354.07"
],
"type": "Person"
},
{
"affiliation": {
"alternateName": "Egerton University",
"id": "https://www.grid.ac/institutes/grid.8301.a",
"name": [
"Institute of Food Nutrition and Safety, School of Food Science and Technology, Jiangnan University, 214122, Wuxi, Jiangsu Province, China",
"Human Nutrition Department, Egerton University, PO BOX 536, Egerton, Kenya"
],
"type": "Organization"
},
"familyName": "Cheserek",
"givenName": "Maureen Jepkorir",
"id": "sg:person.0752303530.29",
"sameAs": [
"https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.0752303530.29"
],
"type": "Person"
},
{
"affiliation": {
"alternateName": "Jiangnan University",
"id": "https://www.grid.ac/institutes/grid.258151.a",
"name": [
"The State Key Laboratory of Food Science and Technology, Jiangnan University, 214122, Wuxi, Jiangsu Province, China",
"Institute of Food Nutrition and Safety, School of Food Science and Technology, Jiangnan University, 214122, Wuxi, Jiangsu Province, China"
],
"type": "Organization"
},
"familyName": "Su",
"givenName": "GuanFang",
"id": "sg:person.01326141366.23",
"sameAs": [
"https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.01326141366.23"
],
"type": "Person"
},
{
"affiliation": {
"alternateName": "Jiangnan University",
"id": "https://www.grid.ac/institutes/grid.258151.a",
"name": [
"The State Key Laboratory of Food Science and Technology, Jiangnan University, 214122, Wuxi, Jiangsu Province, China",
"Institute of Food Nutrition and Safety, School of Food Science and Technology, Jiangnan University, 214122, Wuxi, Jiangsu Province, China"
],
"type": "Organization"
},
"familyName": "Le",
"givenName": "GuoWei",
"id": "sg:person.016101750457.19",
"sameAs": [
"https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.016101750457.19"
],
"type": "Person"
}
],
"citation": [
{
"id": "https://doi.org/10.1016/j.ijantimicag.2011.07.012",
"sameAs": [
"https://app.dimensions.ai/details/publication/pub.1001310061"
],
"type": "CreativeWork"
},
{
"id": "https://doi.org/10.1016/j.peptides.2009.05.016",
"sameAs": [
"https://app.dimensions.ai/details/publication/pub.1001705624"
],
"type": "CreativeWork"
},
{
"id": "https://doi.org/10.1016/j.bbamem.2007.01.005",
"sameAs": [
"https://app.dimensions.ai/details/publication/pub.1002134931"
],
"type": "CreativeWork"
},
{
"id": "https://doi.org/10.1016/0022-2836(67)90353-1",
"sameAs": [
"https://app.dimensions.ai/details/publication/pub.1003427297"
],
"type": "CreativeWork"
},
{
"id": "https://doi.org/10.1016/j.peptides.2006.01.006",
"sameAs": [
"https://app.dimensions.ai/details/publication/pub.1004647093"
],
"type": "CreativeWork"
},
{
"id": "https://doi.org/10.1016/j.foodchem.2008.12.102",
"sameAs": [
"https://app.dimensions.ai/details/publication/pub.1012187672"
],
"type": "CreativeWork"
},
{
"id": "https://app.dimensions.ai/details/publication/pub.1012289284",
"type": "CreativeWork"
},
{
"id": "https://doi.org/10.1016/j.chemphyslip.2010.03.009",
"sameAs": [
"https://app.dimensions.ai/details/publication/pub.1012374137"
],
"type": "CreativeWork"
},
{
"id": "https://doi.org/10.1155/2011/414729",
"sameAs": [
"https://app.dimensions.ai/details/publication/pub.1013433545"
],
"type": "CreativeWork"
},
{
"id": "sg:pub.10.1007/s11434-007-0117-0",
"sameAs": [
"https://app.dimensions.ai/details/publication/pub.1015387701",
"https://doi.org/10.1007/s11434-007-0117-0"
],
"type": "CreativeWork"
},
{
"id": "https://doi.org/10.1016/s0304-4157(98)00014-8",
"sameAs": [
"https://app.dimensions.ai/details/publication/pub.1015707032"
],
"type": "CreativeWork"
},
{
"id": "https://doi.org/10.1006/mthe.2002.0523",
"sameAs": [
"https://app.dimensions.ai/details/publication/pub.1016004169"
],
"type": "CreativeWork"
},
{
"id": "https://doi.org/10.1016/j.febslet.2007.01.086",
"sameAs": [
"https://app.dimensions.ai/details/publication/pub.1020628216"
],
"type": "CreativeWork"
},
{
"id": "https://doi.org/10.1016/j.peptides.2009.09.011",
"sameAs": [
"https://app.dimensions.ai/details/publication/pub.1020867397"
],
"type": "CreativeWork"
},
{
"id": "https://doi.org/10.3390/ijms13033394",
"sameAs": [
"https://app.dimensions.ai/details/publication/pub.1022191542"
],
"type": "CreativeWork"
},
{
"id": "https://doi.org/10.1073/pnas.75.9.4194",
"sameAs": [
"https://app.dimensions.ai/details/publication/pub.1025649906"
],
"type": "CreativeWork"
},
{
"id": "https://doi.org/10.1016/j.febslet.2006.04.078",
"sameAs": [
"https://app.dimensions.ai/details/publication/pub.1026335332"
],
"type": "CreativeWork"
},
{
"id": "https://doi.org/10.1016/j.bbamem.2010.06.016",
"sameAs": [
"https://app.dimensions.ai/details/publication/pub.1031282913"
],
"type": "CreativeWork"
},
{
"id": "https://doi.org/10.1002/psc.1120",
"sameAs": [
"https://app.dimensions.ai/details/publication/pub.1033404374"
],
"type": "CreativeWork"
},
{
"id": "https://doi.org/10.1016/s0167-4838(02)00373-4",
"sameAs": [
"https://app.dimensions.ai/details/publication/pub.1033535144"
],
"type": "CreativeWork"
},
{
"id": "https://doi.org/10.1016/j.bbamem.2007.06.013",
"sameAs": [
"https://app.dimensions.ai/details/publication/pub.1033632501"
],
"type": "CreativeWork"
},
{
"id": "https://doi.org/10.1096/fj.03-0449fje",
"sameAs": [
"https://app.dimensions.ai/details/publication/pub.1033693695"
],
"type": "CreativeWork"
},
{
"id": "https://doi.org/10.1006/bbrc.1998.8159",
"sameAs": [
"https://app.dimensions.ai/details/publication/pub.1034817946"
],
"type": "CreativeWork"
},
{
"id": "https://doi.org/10.1016/j.addr.2007.09.003",
"sameAs": [
"https://app.dimensions.ai/details/publication/pub.1037425494"
],
"type": "CreativeWork"
},
{
"id": "https://doi.org/10.1002/cyto.990010108",
"sameAs": [
"https://app.dimensions.ai/details/publication/pub.1039213158"
],
"type": "CreativeWork"
},
{
"id": "https://doi.org/10.1002/cyto.990010108",
"sameAs": [
"https://app.dimensions.ai/details/publication/pub.1039213158"
],
"type": "CreativeWork"
},
{
"id": "https://doi.org/10.1093/nar/gkl298",
"sameAs": [
"https://app.dimensions.ai/details/publication/pub.1042941044"
],
"type": "CreativeWork"
},
{
"id": "https://doi.org/10.1016/j.clim.2009.12.004",
"sameAs": [
"https://app.dimensions.ai/details/publication/pub.1044494467"
],
"type": "CreativeWork"
},
{
"id": "https://doi.org/10.1016/j.bbamem.2008.09.013",
"sameAs": [
"https://app.dimensions.ai/details/publication/pub.1044725041"
],
"type": "CreativeWork"
},
{
"id": "https://doi.org/10.1093/jac/dkn436",
"sameAs": [
"https://app.dimensions.ai/details/publication/pub.1048316673"
],
"type": "CreativeWork"
},
{
"id": "https://doi.org/10.1016/j.ijantimicag.2005.11.014",
"sameAs": [
"https://app.dimensions.ai/details/publication/pub.1049185656"
],
"type": "CreativeWork"
},
{
"id": "sg:pub.10.1007/s002840010263",
"sameAs": [
"https://app.dimensions.ai/details/publication/pub.1049218355",
"https://doi.org/10.1007/s002840010263"
],
"type": "CreativeWork"
},
{
"id": "https://doi.org/10.1093/nar/6.9.3093",
"sameAs": [
"https://app.dimensions.ai/details/publication/pub.1049243262"
],
"type": "CreativeWork"
},
{
"id": "https://doi.org/10.3390/ph3030448",
"sameAs": [
"https://app.dimensions.ai/details/publication/pub.1051502467"
],
"type": "CreativeWork"
},
{
"id": "https://doi.org/10.1016/s0304-4165(00)00122-7",
"sameAs": [
"https://app.dimensions.ai/details/publication/pub.1053000328"
],
"type": "CreativeWork"
},
{
"id": "https://doi.org/10.1016/s0304-4165(00)00122-7",
"sameAs": [
"https://app.dimensions.ai/details/publication/pub.1053000328"
],
"type": "CreativeWork"
},
{
"id": "https://app.dimensions.ai/details/publication/pub.1074544757",
"type": "CreativeWork"
}
],
"datePublished": "2013-02",
"datePublishedReg": "2013-02-01",
"description": "A number of research have proven that antimicrobial peptides are of greatest potential as a new class of antibiotics. Antimicrobial peptides and cell-penetrating peptides share some similar structure characteristics. In our study, a new peptide analog, APP (GLARALTRLLRQLTRQLTRA) from the cell-penetrating peptide ppTG20 (GLFRALLRLLRSLWRLLLRA), was identified simultaneously with the antibacterial mechanism of APP against Salmonella typhimurium and Streptococcus pyogenes. APP displayed potent antibacterial activity against Gram-negative and Gram-positive strains. The minimum inhibitory concentration was in the range of 2 to 4\u00a0\u03bcM. APP displayed higher cell selectivity (about 42-fold increase) as compared to the parent peptide for it decreased hemolytic activity and increased antimicrobial activity. The calcein leakage from egg yolk L-\u03b1-phosphatidylcholine (EYPC)/egg yolk L-\u03b1-phosphatidyl-DL-glycerol and EYPC/cholesterol vesicles demonstrated that APP exhibited high selectivity. The antibacterial mechanism analysis indicated that APP induced membrane permeabilization in a kinetic manner for membrane lesions allowing O-nitrophenyl-\u03b2-D-galactoside uptake into cells and potassium release from APP-treated cells. Flow cytometry analysis demonstrated that APP induced bacterial live cell membrane damage. Circular dichroism, fluorescence spectra, and gel retardation analysis confirmed that APP interacted with DNA and intercalated into the DNA base pairs after penetrating the cell membrane. Cell cycle assay showed that APP affected DNA synthesis in the cell. Our results suggested that peptides derived from the cell-penetrating peptide have the potential for antimicrobial agent development, and APP exerts its antibacterial activity by damaging bacterial cell membranes and binding to bacterial DNA to inhibit cellular functions, ultimately leading to cell death.",
"genre": "research_article",
"id": "sg:pub.10.1007/s00253-012-4352-1",
"inLanguage": [
"en"
],
"isAccessibleForFree": false,
"isFundedItemOf": [
{
"id": "sg:grant.4982679",
"type": "MonetaryGrant"
},
{
"id": "sg:grant.6987036",
"type": "MonetaryGrant"
}
],
"isPartOf": [
{
"id": "sg:journal.1083533",
"issn": [
"0175-7598",
"1432-0614"
],
"name": "Applied Microbiology and Biotechnology",
"type": "Periodical"
},
{
"issueNumber": "4",
"type": "PublicationIssue"
},
{
"type": "PublicationVolume",
"volumeNumber": "97"
}
],
"name": "Antibacterial activity and dual mechanisms of peptide analog derived from cell-penetrating peptide against Salmonella typhimurium and Streptococcus pyogenes",
"pagination": "1711-1723",
"productId": [
{
"name": "readcube_id",
"type": "PropertyValue",
"value": [
"906128d6b88e39bee8b753bfb13c2d5a9652ca2577a15b750cd1ed7a361e3bb1"
]
},
{
"name": "pubmed_id",
"type": "PropertyValue",
"value": [
"22923068"
]
},
{
"name": "nlm_unique_id",
"type": "PropertyValue",
"value": [
"8406612"
]
},
{
"name": "doi",
"type": "PropertyValue",
"value": [
"10.1007/s00253-012-4352-1"
]
},
{
"name": "dimensions_id",
"type": "PropertyValue",
"value": [
"pub.1030307813"
]
}
],
"sameAs": [
"https://doi.org/10.1007/s00253-012-4352-1",
"https://app.dimensions.ai/details/publication/pub.1030307813"
],
"sdDataset": "articles",
"sdDatePublished": "2019-04-11T02:01",
"sdLicense": "https://scigraph.springernature.com/explorer/license/",
"sdPublisher": {
"name": "Springer Nature - SN SciGraph project",
"type": "Organization"
},
"sdSource": "s3://com-uberresearch-data-dimensions-target-20181106-alternative/cleanup/v134/2549eaecd7973599484d7c17b260dba0a4ecb94b/merge/v9/a6c9fde33151104705d4d7ff012ea9563521a3ce/jats-lookup/v90/0000000001_0000000264/records_8700_00000513.jsonl",
"type": "ScholarlyArticle",
"url": "http://link.springer.com/10.1007%2Fs00253-012-4352-1"
}
]Download the RDF metadata as: json-ld nt turtle xml License info
JSON-LD is a popular format for linked data which is fully compatible with JSON.
curl -H 'Accept: application/ld+json' 'https://scigraph.springernature.com/pub.10.1007/s00253-012-4352-1'
N-Triples is a line-based linked data format ideal for batch operations.
curl -H 'Accept: application/n-triples' 'https://scigraph.springernature.com/pub.10.1007/s00253-012-4352-1'
Turtle is a human-readable linked data format.
curl -H 'Accept: text/turtle' 'https://scigraph.springernature.com/pub.10.1007/s00253-012-4352-1'
RDF/XML is a standard XML format for linked data.
curl -H 'Accept: application/rdf+xml' 'https://scigraph.springernature.com/pub.10.1007/s00253-012-4352-1'
This table displays all metadata directly associated to this object as RDF triples.
243 TRIPLES
21 PREDICATES
72 URIs
29 LITERALS
17 BLANK NODES