| pubmed-article:9675169 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9675169 | lifeskim:mentions | umls-concept:C0013227 | lld:lifeskim |
| pubmed-article:9675169 | lifeskim:mentions | umls-concept:C0380603 | lld:lifeskim |
| pubmed-article:9675169 | lifeskim:mentions | umls-concept:C0596087 | lld:lifeskim |
| pubmed-article:9675169 | lifeskim:mentions | umls-concept:C1704675 | lld:lifeskim |
| pubmed-article:9675169 | lifeskim:mentions | umls-concept:C0349590 | lld:lifeskim |
| pubmed-article:9675169 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:9675169 | pubmed:dateCreated | 1998-8-25 | lld:pubmed |
| pubmed-article:9675169 | pubmed:abstractText | PNU145156E (7,7-(carbonyl-bis[imino-N-methyl-4, 2-pyrrolecarbonylimino[N-methyl-4,2-pyrrole]-carbonylimino]) -bis-(1, 3-naphthalene disulfonate)) is a naphthalene sulfonic distamycin A derivative that interacts with heparin-binding growth factors. Because PNU145156E inhibits tumor angiogenesis, it was selected for clinical development. Picosecond time-resolved fluorescence emission and anisotropy were used to characterize the binding of PNU145156E to the basic fibroblast growth factor (a protein associated with tumor angiogenesis). A decrease in PNU145156E fluorescence lifetime was observed as a function of human basic fibroblast growth factor (bFGF) concentration. Nonlinear least-squares fitting of the binding isotherm yielded Kd = 145 nM for a single class of binding sites. Time-resolved anisotropy gave Kd = 174 nM. Kd = 150 nM was independently verified by quantitative high-performance affinity chromatography. The displaced volume of the complex, calculated from its rotational correlation time, fitted a sphere of 1:1 stoichiometry. These results account for the formation of a tight yet reversible PNU145156E:bFGF complex. An evaluation of PNU145156E fluorescence lifetimes in various solvents has highlighted the forces involved in stabilizing the complex. These are mostly electrostatic-hydrophobic in nature, with a relatively low contribution from hydrogen bonding. Both polar and nonpolar groups are involved on the protein-binding site within a largely hydrophobic cleft. A potential binding trajectory, based on a combination of these results with site-directed chemical modification and known bFGF x-ray structure, is suggested. | lld:pubmed |
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| pubmed-article:9675169 | pubmed:language | eng | lld:pubmed |
| pubmed-article:9675169 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9675169 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:9675169 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:9675169 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9675169 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:9675169 | pubmed:issn | 0006-3495 | lld:pubmed |
| pubmed-article:9675169 | pubmed:author | pubmed-author:ZamahNN | lld:pubmed |
| pubmed-article:9675169 | pubmed:author | pubmed-author:ParolaA HAH | lld:pubmed |
| pubmed-article:9675169 | pubmed:author | pubmed-author:PinetCC | lld:pubmed |
| pubmed-article:9675169 | pubmed:author | pubmed-author:PinesEE | lld:pubmed |
| pubmed-article:9675169 | pubmed:author | pubmed-author:CaiolfaV RVR | lld:pubmed |
| pubmed-article:9675169 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9675169 | pubmed:volume | 75 | lld:pubmed |
| pubmed-article:9675169 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9675169 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9675169 | pubmed:pagination | 672-82 | lld:pubmed |
| pubmed-article:9675169 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:9675169 | pubmed:meshHeading | pubmed-meshheading:9675169-... | lld:pubmed |
| pubmed-article:9675169 | pubmed:year | 1998 | lld:pubmed |
| pubmed-article:9675169 | pubmed:articleTitle | Nature of interaction between basic fibroblast growth factor and the antiangiogenic drug 7,7-(Carbonyl-bis[imino-N-methyl-4, 2-pyrrolecarbonylimino[N-methyl-4,2-pyrrole]-carbonylimino] )bis-(1, 3-naphthalene disulfonate). | lld:pubmed |
| pubmed-article:9675169 | pubmed:affiliation | Department of Oncology, Preclinical Research, Pharmacia & Upjohn, 20014 Nerviano, Milan, Italy. | lld:pubmed |
| pubmed-article:9675169 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:9675169 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:9675169 | lld:pubmed |
