Handedness preference and switching of peptide helices. Part II: Helices based on noncoded α-amino acids

被引：49

作者：

Crisma, Marco ^{[1
]}

De Zotti, Marta ^{[2
]}

Formaggio, Fernando ^{[1
,2
]}

Peggion, Cristina ^{[2
]}

Moretto, Alessandro ^{[1
,2
]}

Toniolo, Claudio ^{[1
,2
]}

机构：

[1] CNR, ICB, Padova Unit, Padua, Italy

[2] Univ Padua, Dept Chem, I-35131 Padua, Italy

来源：

JOURNAL OF PEPTIDE SCIENCE | 2015年 / 21卷 / 03期

关键词：

chirality; handedness; helical structures; nuclear magnetic resonance; peptides; X-ray diffraction crystallography; spectroscopy; switches; SCREW-SENSE PREFERENCE; INACTIVE 3(10)-HELICAL PEPTIDE; VIBRATIONAL CIRCULAR-DICHROISM; PEPTOID SECONDARY STRUCTURE; SOLID-STATE CONFORMATION; CHAIN-LENGTH DEPENDENCE; TERMINAL ELECTRON-DONOR; CHARGE-TRANSFER COMPLEX; N-SUBSTITUTED GLYCINES; AROMATIC SIDE-CHAINS;

D O I：

10.1002/psc.2743

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：

In this second part of our review article on the preferred screw sense and interconversion of peptide helices, we discuss the most significant computational and experimental data published on helices formed by the most extensively investigated categories of noncoded -amino acids. They are as follows: (i) N-alkylated Gly residues (peptoids), (ii) C-alkylated -amino acids, (iii) C-,C--sp(2) configurated -amino acids, and (iv) combinations of residues of types (ii) and (iii). With confidence, the large body of interesting papers examined and classified in this editorial effort will stimulate the development of helical peptides in many diverse areas of biosciences and nanosciences. Copyright (c) 2015 European Peptide Society and John Wiley & Sons, Ltd.

引用

页码：148 / 177

页数：30

共 459 条

[1] Observation of glycine zipper and unanticipated occurrence of ambidextrous helices in the crystal structure of a chiral undecapeptide [J].