The Investigations Of Smart Surface Properties
THE INVESTIGATIONS OF SMART SURFACE PROPERTIES
P. Staszczuk, M. Planda
Department of Physicochemistry of Solid Surface, Faculty of Chemistry,
Maria Curie-Sklodowska University,
Maria Curie-Sklodowska sq. 3, 20-031 Lublin, Poland
The ability of proteins, as highly chiral species, to exhibit enantioselectivity in their binding of certain ligands is knows very well for many years. Studies of the stereodifferentiating properties of proteins with respect to low molecular weight compounds have been performed by a variety of techniques for the determination of protein – ligand equilibria. A logical extension of the method of gel filtration is the use of protein immobilized on a suitable support, a technique introduced in 1973 by Steward and Doherty [1]. Many protein-bonded stationary phases have been developed for resolution of enantiomeres [2]. Those include albumins such as bovine serum albumin (BSA) and human serum albumin (HAS) [3], glycoproteines such as α1–acid glycoprotein, avidin, cellulase [4] and ovoglycoprotein [5], and enzymes such as trypsin, α-chymotrypsin and pepsin. With the implementation of techniques and affinity chromatographic applications [4] proteins were bonded to different support matrices such as agarose, polyacrylamide gel, and silica [1]. We have designed a new HPLC enantioselective material based upon a covalently immobilized BSA on alumina samples.
Enantiomers separations is one of the most important areas in chemistry. In the past decades several kinds of chiral stationary phases have been developed based on the various chiral selector such as celluloses, cyclodextrines, syntetic enantiomers, syntetic polymers and proteins. This study presents a method of synthezing the net protein chiral stationary phases so-called smart surfaces. It has been proved that the protein chiral stationary phases covalently bonded to support matrices such as agarose, silica gel [7,8] possess good stereoselectivity in resolving varies enantiomers because of complex and changeable conformations of bonded protein. Those materials were prepared by chemically attaching bovine serum albumin (BSA) to three different alumina samaples via a three-step process. The alumina samples were
obtained from Aldrich Co. The process consisted of an initial derivatization to yield an aminopropyl-modified alumina flowed by protein coupling with glutaric dialdehyde. The degree of surface coverage at each step was determined by microelemental analysis of carbon and nitrogen. Different kinds of enantiomers were separated successfully on aminopropylalumina-bonded BSA chiral phase. The isotherm of adsorption-desoroption of nitroges on modified aluminaalumina samples were measured using sorptomatic method (aparatus type ASAP 2405 V1.01, Micrometrics Inc., USA) and specific surface area, pore size and volume and pore-size distribution function have been calculated.
References
1. K.K. Steward and R.F. Doherty, Proc. Nat. Acad. Sci. U. S., 70 (1973) 2850.
2. S.R. Narayanaa, J. Pharm. Biomed. Anal., 10 (1992) 251 and references cited therein.
3. Domenici, C. Bertucci, P. Salvadori, G. Felix, I. Cahagne, S. Montellier and I. W. Wainer, Chromatographia, 29 (1990) 170.
4. P. Erlandsson, I. Marle, L. Hansson, R. Isaksson, C. Pettersson and G.Pettersson, J. Am. Chem. Soc., 112 (1990) 4573.
5. J. Haginaka, C. Seyama and N. Kanasugi, Anal. Chem., 67 (1995) 2539.
6. J. Haginaka, N. Kanasugi, J. Chromatogr. A, 708 (1995) 161.
7. P. Staszczuk, Colloids Surf., 94 (1995) 213.
8. P. Staszczuk, J. Thermal Anal., 48 (1997) 755.
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