Abstract
The molecular design to mimic the metal-binding site of a protein molecule entails abstracting the minimum requirements which must be retained in a molecule in order to maintain parameters controling the geometry, metal-binding ligands and microenvironment at the metal-binding site. A linear peptide may be designed to mimic a site which is located on a short linear amino acid sequence. However, when the metal-binding ligands originate from different parts of the polypeptide backbone, a cyclic peptide should be designed with amino acid residues having appropriate side chains. For the purpose of the design, building of suitable molecular models are essential. This can be supplemented by conformational calculations. Three examples are presented for the molecular design of the metal-binding sites: Copper(II)-transport site of human albumin, Zn(II)-binding sites of two metalloenzymes: carboxypeptidase and carbonic anhydrase.
This is a preview of subscription content, log in via an institution to check access.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
Reference
Deber, C.M., Madison, V., and Blout, E.R.: 1976, Accounts Chem. Res. 9, pp. 106–113.
Ramachandran, G.N. and Chandrasekharan, V.: 1972, Progress in Peptide Research, Ed. S. Lande, Gordon and Beach Science Publishers Inc., New York, Vol. 2, pp. 195–215.
Pieroni, O., Montagnoti, G., Fissi, A., Merlino, S., and Ciardelli, F.: 1975, J. Amer. Chem. Soc. 97, pp. 6820–6826.
Peters, T., Jr. and Blumenstock, F.A.: 1967, J. BioZ. Chem. 242, pp. 1574–1578.
Appleton, D.W. and Sarkar, B.: 1971, J. Biol. Chem. 246, pp. 5040–5046.
Dixon, J.W. and Sarkar, B.: 1965, J. BioZ. Chem. 240, pp. 5972–5977.
Lau, S., Kruck, T.P.A., and Sarkar, B.: 1974, J. BioZ. Chem. 249, pp. 5878–5884.
Lau, S. and Sarkar, B.: 1975, Can. J. Chem. 53, pp. 710–715.
Kruck, T.P.A., Lau, S., and Sarkar, B.: 1976, Can. J. Chem. 54, pp. 1300–1308.
Iyer, K.S.N., Lau, S., Laurie, S.H., and Sarkar, B.: 1978, Biochem. J. 169, pp. 61–69.
Camerman, N., Camerman, A., and Sarkar, B.: 1976, Can. J. Chem. 54, pp. 1309–1316.
Lipscomb, W.N., Hartsuck, J.A., Quiocho, F.A., and Reeke, G.N., Jr.: 1969, Proc. Nat. Acad. Sci. USA 64, pp. 28–35.
Kannan, K.K., Notstrand, B., Fridborg, K., Lövgren, S., Ohlsson, A., and Petef, M.: 1975, Proc. Nat. Acad. Sci. USA 72, pp. 51–55.
Appleton, D.W. and Sarkar, B.: 1974, Proc. Nat. Acad. Sci. USA 71, pp. 1686–1690.
Demoulin, D., Pullman, A., and Sarkar, B.: 1977, J. Amer. Chem. Soc. 99, pp. 8498–8500.
Appendix
Sarkar, B.: 1977, Concept of molecular design in relation to the metal-binding sites of proteins and enzymes in Metal-Ligand Interaction in Organic Chemistry and Biochemistry, Ed. B. Pullman and N. Goldblum, Part 1, pp. 193–228 by D. Reidel Publishing Company, Dordrecht-Holland.
Freeman, H.C.: 1967, Crystal structures of metal-peptide complexes in Adv. Protein Chem. 22, pp. 258–424.
Pullman, B. and Pullman, A.: 1974, Molecular orbital calculations on the conformation of amino acid residues of protein in Adv. Protein Chem. 28, pp. 348–526.
Anfinsen, C.B. and Scheraga, H.A.: 1975, Experimental and theoretical aspects of protein folding in Adv. Protein Chem. 29, pp. 205–300.
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1980 D. Reidel Publishing Company
About this chapter
Cite this chapter
Sarkar, B. (1980). Design of Peptide Molecules to Mimic the Metal Binding Sites of Proteins. In: Braibanti, A. (eds) Bioenergetics and Thermodynamics: Model Systems. NATO Advance Study Institutes Series, vol 55. Springer, Dordrecht. https://doi.org/10.1007/978-94-009-9035-7_2
Download citation
DOI: https://doi.org/10.1007/978-94-009-9035-7_2
Publisher Name: Springer, Dordrecht
Print ISBN: 978-94-009-9037-1
Online ISBN: 978-94-009-9035-7
eBook Packages: Springer Book Archive