| pubmed-article:8615847 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8615847 | lifeskim:mentions | umls-concept:C0023767 | lld:lifeskim |
| pubmed-article:8615847 | lifeskim:mentions | umls-concept:C0023810 | lld:lifeskim |
| pubmed-article:8615847 | lifeskim:mentions | umls-concept:C0032535 | lld:lifeskim |
| pubmed-article:8615847 | lifeskim:mentions | umls-concept:C1704675 | lld:lifeskim |
| pubmed-article:8615847 | lifeskim:mentions | umls-concept:C0162621 | lld:lifeskim |
| pubmed-article:8615847 | lifeskim:mentions | umls-concept:C2603343 | lld:lifeskim |
| pubmed-article:8615847 | lifeskim:mentions | umls-concept:C0037791 | lld:lifeskim |
| pubmed-article:8615847 | pubmed:dateCreated | 1996-6-6 | lld:pubmed |
| pubmed-article:8615847 | pubmed:abstractText | Lipopolysaccharide (LPS), the major cell wall constituent of Gram-negative bacteria, evokes a multitude of biological effects in mammals including pyrogenicity and toxic shock syndrome. Polymyxin B (PmB), a polycationic cyclic peptide, is known to neutralize most of its activities. The nature of the interaction of PmB with LPS and lipid A was investigated by isothermal titration calorimetry. PmB binds to LPS as well as lipid A stoichiometrically and non-co-operatively with micromolar affinity. These interactions are driven primarily by a favourable change in entropy (delta S) and are endothermic in nature. These positive changes in enthalpies decrease with increasing temperature, yielding a heat capacity change, delta Cp, of -2385 J.mol-1.degree-1 for PmB-LPS interactions while the binding of PmB to lipid A displays a delta Cp of -2259 J.mol-1.degree-1. The negative heat capacity changes provide strong evidence for the role of hydrophobic interactions as the driving force for the association of PmB with LPS and lipid A. A correlation of the energetics of these interactions with analyses of the molecular models of PmB suggests that a cluster of solvent-exposed non-polar amino acid side-chains that line one surface of the molecule, together with a ring of positively charged residues on its other surface, are responsible for its strong and stoichiometric binding to LPS. | lld:pubmed |
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| pubmed-article:8615847 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8615847 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8615847 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:8615847 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8615847 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:8615847 | pubmed:issn | 0264-6021 | lld:pubmed |
| pubmed-article:8615847 | pubmed:author | pubmed-author:SuroliaAA | lld:pubmed |
| pubmed-article:8615847 | pubmed:author | pubmed-author:Balasubramani... | lld:pubmed |
| pubmed-article:8615847 | pubmed:author | pubmed-author:SuroliaNN | lld:pubmed |
| pubmed-article:8615847 | pubmed:author | pubmed-author:SrimalSS | lld:pubmed |
| pubmed-article:8615847 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8615847 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:8615847 | pubmed:volume | 315 ( Pt 2) | lld:pubmed |
| pubmed-article:8615847 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8615847 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8615847 | pubmed:pagination | 679-86 | lld:pubmed |
| pubmed-article:8615847 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:8615847 | pubmed:year | 1996 | lld:pubmed |
| pubmed-article:8615847 | pubmed:articleTitle | Titration calorimetric studies to elucidate the specificity of the interactions of polymyxin B with lipopolysaccharides and lipid A. | lld:pubmed |
| pubmed-article:8615847 | pubmed:affiliation | Molecular Biophysics Unit, Indian Institute of Science, Bangalore, India. | lld:pubmed |
| pubmed-article:8615847 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8615847 | pubmed:publicationType | In Vitro | lld:pubmed |
| pubmed-article:8615847 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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