Helix induction potential of N-terminal α-methyl, α-amino acids

被引：7

作者：

Gobbo, M

Biondi, L

Filira, F

Formaggio, F

Crisma, M

Rocchi, R

Toniolo, C

Broxterman, QB

Kamphuis, J

机构：

[1] Univ Padua, Dept Organ Chem, CNR, Biopolymer Res Ctr, I-35131 Padua, Italy

[2] DSM Res BV, Organ Chem & Biotechnol Sect, NL-6160 MD Geleen, Netherlands

[3] DSM Fine Chem, NL-6401 JH Heerlen, Netherlands

来源：

LETTERS IN PEPTIDE SCIENCE | 1998年 / 5卷 / 2-3期

关键词：

alpha-aminoisobutyric acid peptides; circular dichroism; conformational analysis; isovaline peptides; C-peptide;

D O I：

10.1023/A:1008873910529

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：

A series of longer analogues of the C-peptide of RNAse A has been synthesized with the aim of assessing the helix induction potential in water of alpha-methyl, alpha-amino acids at the N-terminus of the chain. The circular dichroism data indicate that one isovaline residue is effective in increasing the helix content of the 13-residue peptide by about 7%.

引用

页码：105 / 107

页数：3

共 8 条

[1] ((9-FLUORENYLMETHYL)OXY)CARBONYL (FMOC) AMINO-ACID FLUORIDES - CONVENIENT NEW PEPTIDE COUPLING REAGENTS APPLICABLE TO THE FMOC/TERT-BUTYL STRATEGY FOR SOLUTION AND SOLID-PHASE SYNTHESES [J].