Sequential glycopeptides (Thr(β-d-galactose)-Ala-Ala]n, with n ranging from 2 to 7, as models of natural antifreeze glycoproteins were synthesized by the continuous flow, solid phase procedure. The conformational properties of these materials in solution were investigated by c.d. and 1H-n.m.r. spectroscopy. In aqueous solution the c.d. pattern is practically independent of chain length and is very similar to that of natural antifreeze glycoproteins. The results are interpreted in terms of random coil structure. The absence of ordered structures is further confirmed by n.m.r. data. A small amount of ordered conformation can be induced either by increasing the temperature of the aqueous solution or by addition of TFE. The c.d. pattern of all glycopeptides in water at temperatures higher than 50°C are compatible with the presence of a small amount of α-helix or 310 helix. Since the glyco-hexapeptide is too short to form an α-helix, the hypothesis is made that in the glycopeptides in water at high temperature a small amount of 310 helix is formed. The same is observed for the 21-residue glycopeptide in presence of 85% (v/v) TFE. In this medium, the c.d. data on the glyco-hexapeptide are more compatible with the presence of a small amount of β-structure.

Solid-phase Synthesis and Conformation of Sequential Glycosylated Polytripeptide Sequences Related To Antifreeze Glycoproteins

FILIRA, FERNANDO;BIONDI, LAURA;SCOLARO, BARBARA;MAMMI, STEFANO;PEGGION, EVARISTO;ROCCHI, RANIERO
1990

Abstract

Sequential glycopeptides (Thr(β-d-galactose)-Ala-Ala]n, with n ranging from 2 to 7, as models of natural antifreeze glycoproteins were synthesized by the continuous flow, solid phase procedure. The conformational properties of these materials in solution were investigated by c.d. and 1H-n.m.r. spectroscopy. In aqueous solution the c.d. pattern is practically independent of chain length and is very similar to that of natural antifreeze glycoproteins. The results are interpreted in terms of random coil structure. The absence of ordered structures is further confirmed by n.m.r. data. A small amount of ordered conformation can be induced either by increasing the temperature of the aqueous solution or by addition of TFE. The c.d. pattern of all glycopeptides in water at temperatures higher than 50°C are compatible with the presence of a small amount of α-helix or 310 helix. Since the glyco-hexapeptide is too short to form an α-helix, the hypothesis is made that in the glycopeptides in water at high temperature a small amount of 310 helix is formed. The same is observed for the 21-residue glycopeptide in presence of 85% (v/v) TFE. In this medium, the c.d. data on the glyco-hexapeptide are more compatible with the presence of a small amount of β-structure.
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Utilizza questo identificativo per citare o creare un link a questo documento: http://hdl.handle.net/11577/2510199
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