A D-ANTIFREEZE POLYPEPTIDE DISPLAYS THE SAME ACTIVITY AS ITS NATURAL L-ENANTIOMER

被引：29

作者：

WEN, DY ^{[1
]}

LAURSEN, RA ^{[1
]}

机构：

[1] BOSTON UNIV,DEPT CHEM,BOSTON,MA 02215

来源：

FEBS LETTERS | 1993年 / 317卷 / 1-2期

关键词：

D-POLYPEPTIDE; ANTIFREEZE POLYPEPTIDE; ICE; D-ALPHA-HELIX; CIRCULAR DICHROISM;

D O I：

10.1016/0014-5793(93)81485-I

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The D- and L-forms of an alpha-helical antifreeze polypeptide (AFP) have been chemically synthesized. Circular dichroism spectra of the molecules show equal and opposite ellipticities. The D- and the L-enantiomers alone, and a 50:50 mixture of the two, all show identical antifreeze activity, but the enantiomeric forms are predicted to bind to the ice surface with different orientations. It is suggested that symmetry properties of certain ice surfaces permit the asymmetric binding of AFPs, and thus that AFPs are analogous to enzymes that act upon prochiral substrates.

引用

页码：31 / 34

页数：4

共 10 条

[1]

ANATHANARAYANAN VS, 1989, LIFE CHEM REPORTS, V7, P1

[2] ENERGY-OPTIMIZED STRUCTURE OF ANTIFREEZE PROTEIN AND ITS BINDING MECHANISM [J].