Hostname: page-component-586b7cd67f-gb8f7 Total loading time: 0 Render date: 2024-11-30T23:27:54.631Z Has data issue: false hasContentIssue false

New Carbohydrate-Based Polymeric Materials

Published online by Cambridge University Press:  29 November 2013

Get access

Extract

The total world production of water-soluble polymers is estimated to be greater than five million tons per year. Water-soluble polymers are most conveniently described according to their origin in three classes (see Structures 1-6):

∎ Natural polymers, including starch (1) and cellulose (2);

∎ chemically modified natural polymers, including, for example, hydroxyethyl starch (3) and cellulose acetate (4); and

∎ synthetic polymers, the most important of which are polyacrylamide (5) and polyvinyl alcohol (6), (commonly composed of both alcohol and acetate groups as shown). The widespread use of these materials is due to both their availability and the range of useful physical properties found in the various natural and chemically modified natural polymers.

Of the commercial water-soluble polymers, approximately 50–80% are based on natural polysaccharide materials. One of the primary reasons that these materials find such widespread use is the dramatic response of their properties to changes in their functionality and stereochemistry: chemical modification or the combination of polysaccharides with other polymeric materials has yielded materials whose applications range from explosives to food additives. Although efforts directed at controlling the properties of polysaccharides has resulted in a wide variety of useful materials, we felt control of the composition of carbohydrate-based polymers at the molecular level would provide materials with properties superior to those derived from natural and chemically modified polysaccharide materials.

Our approach for the preparation of new carbohydrate-based materials is to use the carbohydrate as a template for the introduction of desired functionality with complete regiochemical and stereochemical control by both chemical and enzymatic methods (Scheme I).

Type
Biology and Materials Synthesis
Copyright
Copyright © Materials Research Society 1992

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)

References

1.Yalpani, M. and Sandford, P.A., in Industrial Polysaccharides, edited by Yalpani, M. (Elsevier, New York, 1987) p. 311.Google Scholar
2.Modified Starches: Properties and Uses; edited by Wurzburg, O.B. (CRC Press, Boca Raton, 1986).Google Scholar
3.New Developments in Industrial Polysaccharides, edited by Crescenzi, V., Dea, I.C.M., and Stivala, S.S. (Gordon and Breach, New York, 1985).Google Scholar
4.Cellulose and Its Derivatives, edited by Kennedy, J.F., Phillips, G.O., Wedlock, D.J., and Williams, P.A. (Wiley and Sons, New York, 1985).Google Scholar
5.Sandford, P.A. and Baird, J., in The Polysaccharides, Vol. II, edited by Aspinall, G.O. (Academic Press, New York, 1983) p. 411.CrossRefGoogle Scholar
6.Kennedy, J.F. and White, C.A., Bioactive Carbohydrates (Ellis Horwood Limited, 1983).Google Scholar
7.Food Hydrocolloids, edited by Glicksman, M. (CRC Press, Boca Raton, 1982).Google Scholar
8.Blanshard, J.M.V. and Mitchell, J.R., Polysaccharides in Food (Butterworths, Boston, 1979).Google Scholar
9.Industrial Gums, edited by Whistler, R.L. (Academic Press, New York, 1973).Google Scholar
10.Mandel, M., in Chemistry and Technology of Water-Soluble Polymers, edited by Finch, C.A. (Plenum, New York, 1983) p. 179.CrossRefGoogle Scholar
11.Hayes, M.E., Nestaas, E., and Hrebenar, K.R., Chemtech 16 (1986) p. 239.Google Scholar
12.Hirschbein, B.L., Mazenod, F.P., and Whitesides, G.M., J. Org. Chem. 47 (1982) p. 3765.CrossRefGoogle Scholar
13.Hill, T.G., Wang, P., Oehler, L.M., Huston, M.E., Wartchow, C.A., Bednarski, M.D., and Callstrom, M.R., Tet. Lett. 32 (1991) p. 6823.CrossRefGoogle Scholar
14.Nakatsuka, T., Sasaki, T., and Kaiser, E.T., J. Am. Chem. Soc. 109 (1987) p. 3808.CrossRefGoogle Scholar
15.Kaiser, E.T., Mihara, H., Laforet, G.A., Kelly, J.W., Walters, L., Findeis, M.A., and Sasaki, T., Science 243 (1989) p. 187.CrossRefGoogle Scholar
16.Barbas, C.F., Matos, J.R., West, J.B., and Wong, C-H., J. Am. Chem. Soc. 110 (1988) p. 5162.CrossRefGoogle Scholar
17.Kitaguchi, H. and Klibanov, A.M., J. Am. Chem. Soc. 111 (1989) p. 9272.CrossRefGoogle Scholar
18.Bergmann, M. and Fraenkel-Conrat, J., J. Biol. Chem. 119 (1937) p. 707.CrossRefGoogle Scholar
19.Bergmann, M. and Fraenkel-Conrat, J., J. Biol. Chem. 124 (1938) p. 1.CrossRefGoogle Scholar
20.Kullman, W., Enzymatic Peptide Synthesis (CRC Press, Boca Raton, 1987).Google Scholar
21.Wang, P., Hill, T.G., Bednarski, M.D., and Callstrom, M.R., Tet. Lett. 32 (1991) p. 6827.CrossRefGoogle Scholar
22.Wang, P., Hill, T.G., Wartchow, C.A., Huston, M.E., Oehler, L.M., Smith, M.B., Bednarski, M.D., and Callstrom, M.R., J. Am. Chem. Soc. 114 (1992) p. 378.CrossRefGoogle Scholar
23.Gray, G.R., Arch. Biochem. Biophys. 163 (1974) p. 426.CrossRefGoogle Scholar
24.Schwartz, B.A. and Gray, G.R., Arch. Biochem. Biophys. 181 (1977) p. 542.CrossRefGoogle Scholar
25.Gray, G.R., Schwartz, B.A., and Kamicker, B.J., Cell Surf. Carbohydr. Biol. Recog. (1978) p. 583.Google Scholar
26.Gray, G.R., Meth. Enz. 50 (1978) p. 155.Google Scholar
27.Roy, R., Katzenellenbogen, E., and Jennings, H.J., Can. J. Biochem. Cell Biol. 62 (1984) p. 270.CrossRefGoogle Scholar
28. The 7-CPC(Protease)—9-CPC(Protease) materials were purified by gel filtration chromatography using 0.05 M sodium borate solution at pH 8 on Sephacryl HR-200 at a flow rate of 1.5 ml/min. Alternatively, isolation by dialysis of the reaction solution using Spectra Por CE 100K MWCO membrane against 2×500 ml of 0.05 M sodium borate at pH 8 for approximately 48 h gave approximately 40% yields for α-chymotrypsin (E.C. 3.4.21.1, Sigma) and trypsin (E.C. 3.4.21.4, Sigma) conjugates and approximately 10% yields (60% recovered activity) for subtilisin BPN′ (Type XXVII, Sigma) conjugates.Google Scholar
29. The kinetic parameters [kcat. Km] for the native enzymes and the CPC analogs are as follows: CT (40s−1, 33 μM), 7-CPC(CT) (46s−1, 20 μM); Try (760s−1, 90 μM), 7-C(Try) (890s−1,1.2 μM); BPN′ (240s−1,83 μM), 7-CPC(BPN′) (350s−1,76 μM).Google Scholar
30.DelMar, E.G., Largman, C., Brodrick, J.W., and Geokas, M.C., Anal. Biochem. 99 (1979) p. 316.CrossRefGoogle Scholar
31.Schonbaum, G.R., Zerner, B., and Bender, M.L., J. Biol. Chem. 236 (1961) p. 2930.CrossRefGoogle Scholar
32.Erlanger, B.F., Kokowsky, N., and Cohen, W., Arch. Biochem. Biophys. 95 (1961) p. 271.CrossRefGoogle Scholar
33.Bender, M.L., Begue-Canton, M.L., Blakeley, R.L., Brubacher, L.J., Feder, J., Gunter, C.R., Kezdy, F.J., Killheffer, J.V. Jr., Marshall, T.H., Miller, C.G., Roeske, R.W., and Stoops, J.K., J. Am. Chem. Soc. 88 (1966) p. 5890.CrossRefGoogle Scholar
34.Thomas, P.G., Russell, A.J., and Fersht, A.R., Nature 318 (1985) p. 375.CrossRefGoogle Scholar