Linked Life Data

16276531

Source:http://linkedlifedata.com/resource/pubmed/id/16276531

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
2006-3-21
pubmed:abstractText
In the present work, the effect of stationary phase resin chemistry and protein physicochemical properties on protein binding affinity in hydrophobic interaction chromatography (HIC) was investigated using linear gradient chromatography and quantitative structure-retention relationship (QSRR) modeling. Linear gradient experiments were carried out for a set of model proteins on four different HIC resins having different backbone and ligand chemistry. The retention data exhibited significant differences in protein binding affinity, not only across the phenyl and butyl ligand chemistries, but also for the different backbone chemistries found in the Sepharose (cross-linked agarose) and the Toyopearl 650 M (polymethacrylate) series of resins. QSRR models based on a Support Vector Machine (SVM) approach were developed for the linear retention data using molecular descriptors based on protein crystal structure and primary sequence information as well as a set of new hydrophobicity descriptors based on the solvent accessible protein surface area. The results indicate that the QSRR models were successfully able to capture and selectivity predict the changes observed in these systems. Furthermore, the new descriptors resulted in physically interpretable models of protein retention and provided insights into the factors influencing protein affinity in these different HIC systems. The approach put forth in this study provides a framework for developing predictive tools and for gaining insight into protein selectivity in hydrophobic interaction chromatography.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0006-3592
pubmed:author
pubmed:copyrightInfo
(c) 2005 Wiley Periodicals, Inc.
pubmed:issnType
Print
pubmed:day
5
pubmed:volume
93
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
836-50
pubmed:dateRevised
2010-11-18
pubmed:meshHeading
pubmed:year
2006
pubmed:articleTitle
Investigation of protein retention and selectivity in HIC systems using quantitative structure retention relationship models.
pubmed:affiliation
Department of Chemical and Biological Engineering, Rensselaer Polytechnic Institute, Troy, New York 12180, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, Non-P.H.S.