当前位置： SCI文献检索 > INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES期刊下所有文献 > Solid phase synthesis and conformation of sequential glycosylated polytripeptide sequences related to antifreeze glycoproteins.

Solid phase synthesis and conformation of sequential glycosylated polytripeptide sequences related to antifreeze glycoproteins.

Abstract：

:Sequential glycopeptides [Thr(beta-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 degrees C are compatible with the presence of a small amount of alpha-helix or 3(10) helix. Since the glyco-hexapeptide is too short to form an alpha-helix, the hypothesis is made that in the glycopeptides in water at high temperature a small amount of 3(10) 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 beta-structure.

journal_name

Int J Biol Macromol

journal_title

International journal of biological macromolecules

authors

Filira F,Biondi L,Scolaro B,Foffani MT,Mammi S,Peggion E,Rocchi R

doi

10.1016/0141-8130(90)90080-t

subject

Has Abstract

pub_date

1990-02-01 00:00:00

pages

41-9

issue

1

eissn

0141-8130

issn

1879-0003

pii

0141-8130(90)90080-T

journal_volume

12

pub_type

杂志文章

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