ISSN:
1573-3904
Keywords:
immunoaffinity chromatography
;
peptide synthesis
;
poly(glycidyl methacrylate-co-ethylene dimethacrylate) monolithic discs
Source:
Springer Online Journal Archives 1860-2000
Topics:
Chemistry and Pharmacology
Notes:
Abstract The preparation method of peptide ligandsemploying polymer-supported solid-phase synthesisand leading to biospecific sorbents has beendesigned and optimized. This approach directlyaffords porous polymer sorbents for biospecificchromatography and avoids the cleavage of thesynthesized peptide moieties from the carrier andtheir isolation. The specifics of both peptidesynthesis and biospecific chromatography usinghydrophilic macroporous polymer supports based onporous poly(glycidyl methacrylate-co-ethylenedimethacrylate) beads and discs were alsoinvestigated. The protecting groups can be removed from the target peptide (bradykinin) attached tothe polymer support by trifluoromethylsulfonic acidwithout any significant loss of the attached peptidefrom the polymer carrier. Introduction of styreneas a comonomer into the copolymer structureimproves the reactivity of the support. However, nononspecific adsorption of proteins in the course ofthe biospecific isolation of antibradykininantibodies was observed with these media. Incontrast, the nonspecific sorption of proteinsincreases as a result of increasing peptide loading.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1023/A:1008933401753
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