Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2005-3-4
pubmed:abstractText
Poly(N-isopropylacrylamide) (PNIPA)-based sorbents have been successfully used as sorbents in temperature-sensitive chromatography. Yet, the mechanisms controlling the binding of biochemicals to these sorbents and, therefore, the separation process are not fully understood. In the current work, the role of hydrophobic interactions in the binding of amino acids of different hydrophobicities to PNIPA microgels was studied. Binding experiments were conducted both below (25 degrees C) and above (37 degrees C) the volume-phase transition temperature of the gel. At 25 degrees C, no straightforward correlation between the partition coefficient and the hydrophobicity could be suggested for low hydrophobicity values. Contrary, at higher hydrophobicities the partition coefficient increases with increasing hydrophobicity. This correlation holds for the whole hydrophobicity range at 37 degrees C; however, the binding data suggests two different binding mechanisms of the hydrophilic amino acids and the hydrophobic ones. Isothermal titration calorimetry measurements confirmed this suggestion: The binding of hydrophobic amino acids seems to be driven by hydrophobic interactions, as evident from the positive binding enthalpy and the clear correlation between the amino acid's hydrophobicity and the binding entropy. Contrary, the binding of the hydrophilic amino acids was exothermic, implying a binding mechanism based on specific interactions, most probably hydrogen bonding.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0743-7463
pubmed:author
pubmed:issnType
Print
pubmed:day
6
pubmed:volume
20
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
169-74
pubmed:dateRevised
2010-11-18
pubmed:meshHeading
pubmed:year
2004
pubmed:articleTitle
Binding of amino acids to "smart" sorbents: where does hydrophobicity come into play?
pubmed:affiliation
Department of Chemical Engineering, Technion-Israel Institute of Technology, Haifa 32000, Israel. bianco@techunix.technion.ac.il
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't