pubmed-article:2554798 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:2554798 | lifeskim:mentions | umls-concept:C0002645 | lld:lifeskim |
pubmed-article:2554798 | lifeskim:mentions | umls-concept:C0002680 | lld:lifeskim |
pubmed-article:2554798 | lifeskim:mentions | umls-concept:C0030956 | lld:lifeskim |
pubmed-article:2554798 | lifeskim:mentions | umls-concept:C0279516 | lld:lifeskim |
pubmed-article:2554798 | lifeskim:mentions | umls-concept:C0301869 | lld:lifeskim |
pubmed-article:2554798 | lifeskim:mentions | umls-concept:C0871161 | lld:lifeskim |
pubmed-article:2554798 | pubmed:issue | 9 | lld:pubmed |
pubmed-article:2554798 | pubmed:dateCreated | 1989-12-12 | lld:pubmed |
pubmed-article:2554798 | pubmed:abstractText | N-Formyl dipeptide conjugates of ampicillin and amoxicillin related to the chemotactic peptide N-formyl-L-methionyl-L-leucyl-L-phenylalanine were synthesized and assessed for antibacterial activity and affinity for the chemotactic peptide receptor of differentiated human promyelocytic leukemia (HL-60) cells. The conjugates and parent beta-lactam antibiotics showed similar antibacterial activities against Escherichia coli and Staphylococcus aureus. The affinity of each conjugate for the chemotactic peptide receptor was determined in a competitive binding assay, using 3H-labeled N-formyl-L-methionyl-L-leucyl-L-phenylalanine. All conjugates bound to the receptor, but with affinities ranging from 1/3 to 1/100 that of the tritiated substrate. There was good correlation between receptor affinity and stimulation of chemotaxis. The peptide-antibiotic conjugates also stimulated the oxidative metabolism of the HL-60 cells by inducing the production of superoxide and hydrogen peroxide as determined by Luminol- and Lucigenin-enhanced chemiluminescence. These conjugates, based on N-formyl-L-methionyl-L-leucyl-L-phenylalanine, thus combine both potent antibacterial and immunostimulatory properties within the same molecule. | lld:pubmed |
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pubmed-article:2554798 | pubmed:language | eng | lld:pubmed |
pubmed-article:2554798 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2554798 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:2554798 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2554798 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2554798 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2554798 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2554798 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2554798 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2554798 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2554798 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:2554798 | pubmed:month | Sep | lld:pubmed |
pubmed-article:2554798 | pubmed:issn | 0066-4804 | lld:pubmed |
pubmed-article:2554798 | pubmed:author | pubmed-author:WilliamsPP | lld:pubmed |
pubmed-article:2554798 | pubmed:author | pubmed-author:BycroftB WBW | lld:pubmed |
pubmed-article:2554798 | pubmed:author | pubmed-author:LockeyP MPM | lld:pubmed |
pubmed-article:2554798 | pubmed:author | pubmed-author:GroutR JRJ | lld:pubmed |
pubmed-article:2554798 | pubmed:author | pubmed-author:PenroseAA | lld:pubmed |
pubmed-article:2554798 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:2554798 | pubmed:volume | 33 | lld:pubmed |
pubmed-article:2554798 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:2554798 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:2554798 | pubmed:pagination | 1516-21 | lld:pubmed |
pubmed-article:2554798 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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pubmed-article:2554798 | pubmed:year | 1989 | lld:pubmed |
pubmed-article:2554798 | pubmed:articleTitle | Antibacterial and immunostimulatory properties of chemotactic N-formyl peptide conjugates of ampicillin and amoxicillin. | lld:pubmed |
pubmed-article:2554798 | pubmed:affiliation | Department of Pharmaceutical Sciences, The University, Nottingham, United Kingdom. | lld:pubmed |
pubmed-article:2554798 | pubmed:publicationType | Journal Article | lld:pubmed |