Linked Life Data

19058882

Source:http://linkedlifedata.com/resource/pubmed/id/19058882

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
2009-3-27
pubmed:abstractText
Fibrin represents a suitable target for addressing delivery systems loaded by fibrinolytic drugs. Selective ligands capable to recognize fibrin could be used as targeting moieties for such systems. In this study the interactions between the gamma(312-324) epitope of human fibrin and peptidic ligands were analyzed by using experimental and computational methods. Binding free energies were calculated through the molecular mechanics/generalized born surface area approach. Good qualitative agreements between the experimental and calculated data were obtained. The binding affinity seems to be well correlated (R(2)=0.69) with the changes of the nonpolar solvation energy term computed from solvent-accessible surface area calculation. These results indicate that current methods of estimating binding free energies are efficient for achieving information on protein-ligand interactions.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
1768-3254
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
44
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2128-34
pubmed:meshHeading
pubmed:year
2009
pubmed:articleTitle
Computational modeling and surface plasmon resonance analyses in the assessment of peptide ligands interacting with fibrin gamma(312-324) epitope.
pubmed:affiliation
BIOlab, UdR INSTM, Department of Chemistry and Industrial Chemistry, University of Pisa, Via Vecchia Livornese 1291, 56122 San Piero a Grado, Pisa, Italy.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't