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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
7
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pubmed:dateCreated |
1991-4-23
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pubmed:abstractText |
Peptides with affinity for opioid receptors were found in an artificially methyl-esterified peptic digest of human lactoferrin. Three active peptides were purified by two steps of reverse-phase high-performance liquid chromatography. Their structures were Tyr-Leu-Gly-Ser-Gly-Tyr-OCH3, Arg-Tyr-Tyr-Gly-Tyr-OCH2, and Lys-Tyr-Leu-Gly-Pro-Gln-Tyr-OCH3, which respectively correspond to the methyl esters of residues 318-323, 536-540, and 673-679 of human lactoferrin. The IC50 values of these peptides were 15, 10 and 23 microM, respectively, in a radioreceptor assay in the presence of 1 nM [3H]naloxone. In the myenteric plexus preparation of the longitudinal muscle of guinea pig ileum, the individual peptides had no opioid agonist activities, but they antagonized [Met5]enkephalin and morphiceptin when they were at a concentration of 10(-6)-10(-5) M, suggesting that these were the opioid antagonist peptides. These three opioid antagonist peptides were named lactoferroxin A, B and C, after casoxin, the opioid antagonist peptide derived from bovine kappa-casein. Concerning the antagonist activities of lactoferroxins for opioid receptor sub-types, lactoferroxin A showed preference for mu-receptors, while lactoferroxin B and C had somewhat higher degrees of preference for kappa-receptors than for mu-receptors. A study of the structure-activity relationship of the three lactoferroxins and their synthetic analogues showed that these opioid antagonist peptides derived from food protein could be expressed by the general formula XA-Tyr-XB-Tyr-OCH3. An amino acid in position XA may affect the specificity of the antagonist peptide for opioid receptor sub-types.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
B
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Lactoferrin,
http://linkedlifedata.com/resource/pubmed/chemical/Narcotic Antagonists,
http://linkedlifedata.com/resource/pubmed/chemical/Oligopeptides,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments,
http://linkedlifedata.com/resource/pubmed/chemical/Peptides,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Opioid
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
0002-1369
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
54
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1803-10
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pubmed:dateRevised |
2011-11-17
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pubmed:meshHeading |
pubmed-meshheading:1369293-Amino Acid Sequence,
pubmed-meshheading:1369293-Humans,
pubmed-meshheading:1369293-Lactoferrin,
pubmed-meshheading:1369293-Molecular Sequence Data,
pubmed-meshheading:1369293-Narcotic Antagonists,
pubmed-meshheading:1369293-Oligopeptides,
pubmed-meshheading:1369293-Peptide Fragments,
pubmed-meshheading:1369293-Peptides,
pubmed-meshheading:1369293-Receptors, Opioid,
pubmed-meshheading:1369293-Structure-Activity Relationship
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pubmed:year |
1990
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pubmed:articleTitle |
Isolation and characterization of opioid antagonist peptides derived from human lactoferrin.
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pubmed:affiliation |
Department of Food Science and Technology, Faculty of Agriculture, Kyoto University, Japan.
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pubmed:publicationType |
Journal Article
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