rdf:type |
|
lifeskim:mentions |
|
pubmed:issue |
11
|
pubmed:dateCreated |
2009-5-19
|
pubmed:abstractText |
Herein we report a series of novel chloramphenicol amine derivatives as aminopeptidase N (APN)/CD13 inhibitors. All compounds were synthesized starting from commercially available (1S,2S)-2-amino-1-(4-nitrophenyl) propane-1,3-diol. The preliminary biological screening showed that some compounds exhibited potent inhibitory activity against APN. It should be noted that one compound, 13b (IC(50)=7.1 microM), possess similar APN inhibitory activity compared with Bestatin (IC(50)=3.0 microM).
|
pubmed:language |
eng
|
pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
|
pubmed:status |
MEDLINE
|
pubmed:month |
Jun
|
pubmed:issn |
1464-3391
|
pubmed:author |
|
pubmed:issnType |
Electronic
|
pubmed:day |
1
|
pubmed:volume |
17
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
3810-7
|
pubmed:meshHeading |
pubmed-meshheading:19423354-Amines,
pubmed-meshheading:19423354-Antigens, CD13,
pubmed-meshheading:19423354-Catalytic Domain,
pubmed-meshheading:19423354-Chloramphenicol,
pubmed-meshheading:19423354-Drug Design,
pubmed-meshheading:19423354-Enzyme Activation,
pubmed-meshheading:19423354-HL-60 Cells,
pubmed-meshheading:19423354-Humans,
pubmed-meshheading:19423354-Inhibitory Concentration 50,
pubmed-meshheading:19423354-Leucine,
pubmed-meshheading:19423354-Models, Biological,
pubmed-meshheading:19423354-Molecular Structure,
pubmed-meshheading:19423354-Protease Inhibitors
|
pubmed:year |
2009
|
pubmed:articleTitle |
Design and synthesis of novel chloramphenicol amine derivatives as potent aminopeptidase N (APN/CD13) inhibitors.
|
pubmed:affiliation |
Department of Medicinal Chemistry, School of Pharmacy, Shandong University, 44 West Culture Road, Ji'nan, Shandong 250012, China.
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|