Size exclusion chromatographic characterization of sodium hyaluronate fractions prepared by high energetic sonication

1993 ◽  
Vol 37 (1-2) ◽  
pp. 20-22 ◽  
Author(s):  
E. Orviský ◽  
L. Šoltés ◽  
P. Chabreček ◽  
I. Novák ◽  
M. Stančíková
Keyword(s):  
Sodium Hyaluronate ◽  
Size Exclusion ◽  
Size Exclusion Chromatographic ◽  
Chromatographic Characterization

scholarly journals Analysis and characterization of dimerization inhibition of a multi-drug-resistant Human Immunodeficiency Virus Type 1 protease using a novel size-exclusion chromatographic approach

2009 ◽  
Vol 419 (2) ◽  
pp. 497-506 ◽  
Author(s):  
David A. Davis ◽  
Irene R. Tebbs ◽  
Sarah I. Daniels ◽  
Stephen J. Stahl ◽  
Joshua D. Kaufman ◽  
...  
Keyword(s):  
Kinetic Analysis ◽  
Active Site ◽  
Active Regions ◽  
Size Exclusion ◽  
Drug Resistant ◽  
Elution Time ◽  
Size Exclusion Chromatographic ◽  
Hiv 1 ◽  
Dimerization Inhibitors

Active-site inhibitors of HIV-1 PR (protease) block viral replication by preventing viral maturation. However, HIV-1 often develops resistance to active-site inhibitors through multiple mutations in PR and therefore recent efforts have focused on inhibiting PR dimerization as an alternative approach. Dimerization inhibitors have been identified using kinetic analysis, but additional characterization of the effect of these inhibitors on PR by physical methods has been difficult. In the present study, we identified a PRMDR (multi-drug-resistant HIV-1 PR) that was highly resistant to autoproteolysis. Using this PR and a novel size-exclusion chromatographic approach that incorporated fluorescence and MS detection, we were able to demonstrate inhibition of dimerization using P27 (peptide 27), a peptide dimerization inhibitor of PR previously identified on the basis of kinetic analysis. Incubation of PRMDR with P27, or other dimerization inhibitors, led to a dose- and time-dependent formation of PR monomers based on the change in elution time by size exclusion and its similar elution time to engineered forms of monomeric PR, namely PRT26A and glutathionylated PR. In contrast, incubation of PRMDR with a potent active-site inhibitor did not change the elution time for the PRMDR dimer. The monomeric PR induced by P27 had fluorescent characteristics which were consistent with unfolded PR. Structure–activity studies identified the active regions of P27 and experiments were performed to examine the effect of other dimerization inhibitors on PR. The present study is the first characterization of dimerization inhibition of PRMDR, a prime target for these inhibitors, using a novel size-exclusion chromatographic approach.

Thin-layer chromatographic characterization of metabolites formed from an AMPA antagonist drug candidate

2001 ◽  
Vol 14 (4) ◽  
pp. 266-271 ◽  
Author(s):  
Katalin Migléczi ◽  
István Hazai ◽  
Katalin Jemnitz ◽  
Márta Pátfalusi
Keyword(s):  
Thin Layer ◽  
Drug Candidate ◽  
Ampa Antagonist ◽  
Chromatographic Characterization
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