Prediction of immobilized artificial membrane-liquid chromatography retention of some drugs from their molecular structure descriptors and LFER parameters

2009 ◽  
Vol 32 (20) ◽  
pp. 3395-3402 ◽  
Author(s):  
Mohammad Hossein Fatemi ◽  
Hoda Shamseddin
Keyword(s):  
Molecular Structure ◽  
Liquid Chromatography ◽  
Artificial Membrane ◽  
Immobilized Artificial Membrane

scholarly journals Immobilized artificial membrane (IAM) liquid chromatography as a model for antimicrobial peptide partitioning into cell membranes: An evaluation

Eureka ◽  
2010 ◽  
Vol 1 (1) ◽  
pp. 20-33
Author(s):  
Matthew Benesch ◽  
Ruthvnen Lewis ◽  
Ronald McElhaney
Keyword(s):  
Liquid Chromatography ◽  
Antimicrobial Peptides ◽  
Lipid Bilayers ◽  
Screening Method ◽  
Interfacial Region ◽  
Artificial Membrane ◽  
Lipid Packing ◽  
Immobilized Artificial Membrane ◽  
Fast Screening ◽  
Packing Densities

Non-covalent immobilized artificial membrane reverse-phase high performance liquid chromatography was previously evaluated as a means whereby elution times for antimicrobial peptides from columns mimicking the lipid bilayers of different membrane systems might be used as a fast-screening method to compare relative binding effectiveness. Such a system would aid in the development of antimicrobial peptides that bind preferentially to model pathogenic systems and leave the host’s membranes reasonably unaffected. A non-covalent approach allows for flexibility in membrane composition but was found to be inadequate for analysis of most peptides due to significant lipid loss at high acetonitrile concentrations. A covalent approach where phosphatidylcholine was amide-linked to the silica surface was examined to evaluate its use as a fast-screening method and compare its data to that collected from the non-covalent columns. Initial work with a 1-cm column proved ineffective due to problems with balancing flow rates with retention times, and work was shifted to a longer 10-cm column. Results suggested that peptides bind much more strongly to covalent columns than non-covalent ones, with the binding especially enhanced by the presence of cationic residues. These columns had lipid packing densities much lower than true membranes, indicating that the peptides were partitioning deep into the bonded phase of the columns rather than into the interfacial region of the phosphate head groups, as expected in situations of biologically-relevant lipid packing densities.

Predicting the phospholipophilicity of monoprotic positively charged amines

2017 ◽  
Vol 19 (3) ◽  
pp. 307-323 ◽  
Author(s):  
S. T. J. Droge ◽  
J. L. M. Hermens ◽  
S. Gutsell ◽  
J. Rabone ◽  
G. Hodges
Keyword(s):  
High Performance Liquid Chromatography ◽  
Liquid Chromatography ◽  
High Performance ◽  
Artificial Membrane ◽  
Immobilized Artificial Membrane ◽  
Phospholipid Monolayers ◽  
Positively Charged

The sorption affinity of eighty-six charged amine structures to phospholipid monolayers (log KIAM) was determined using immobilized artificial membrane high-performance liquid chromatography (IAM-HPLC).

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