Solution conformations of helix-forming β-amino acid homooligomers

被引:118
作者
Barchi, JJ [1 ]
Huang, XL
Appella, DH
Christianson, LA
Durell, SR
Gellman, SH
机构
[1] NCI, Div Basic Sci, Med Chem Lab, Bethesda, MD 20892 USA
[2] NCI, Div Basic Sci, Lab Expt & Computat Biol, Bethesda, MD 20892 USA
[3] Univ Wisconsin, Dept Chem, Madison, WI 53706 USA
关键词
D O I
10.1021/ja9930014
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
The conformational properties of beta-peptides comprised of enantiomerically pure trans-2-aminocyclohexanecarboxylic acid (ACHC) or trans-2-aminocyclopentanecarboxylic acid (ACPC) units were studied by NMR spectroscopy in organic solvents. In pyridine-d(5) solution, ACPC hexamer 1 and ACPC octamer 2 displayed well-defined helical structures characterized by a series of 12-membered hydrogen-bonded rings ("12-helix"). The solution structures calculated from the NMR-derived constraints were very similar to the conformations found previously for 1 and 2 in the solid state. ACHC tetramer 3 displayed a different sort of helical conformation, characterized by a series of 14-membered hydrogen-bonded rings ("14-helix"), in methanol-d(3) solution. This solution conformation is similar to that previously found in the crystal structure of 3.
引用
收藏
页码:2711 / 2718
页数:8
相关论文
共 66 条
[1]  
Abele S, 1998, HELV CHIM ACTA, V81, P2141, DOI 10.1002/(SICI)1522-2675(19981216)81:12<2141::AID-HLCA2141>3.0.CO
[2]  
2-5
[3]   Extracting information from the temperature gradients of polypeptide NH chemical shifts .1. The importance of conformational averaging [J].
Andersen, NH ;
Neidigh, JW ;
Harris, SM ;
Lee, GM ;
Liu, ZH ;
Tong, H .
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 1997, 119 (36) :8547-8561
[4]   Synthesis and structural characterization of helix-forming β-peptides:: trans-2-aminocyclopentanecarboxylic acid oligomers [J].
Appella, DH ;
Christianson, LA ;
Klein, DA ;
Richards, MR ;
Powell, DR ;
Gellman, SH .
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 1999, 121 (33) :7574-7581
[5]   Synthesis and characterization of trans-2-aminocyclohexanecarboxylic acid oligomers:: An unnatural helical secondary structure and implications for β-peptide tertiary structure [J].
Appella, DH ;
Christianson, LA ;
Karle, IL ;
Powell, DR ;
Gellman, SH .
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 1999, 121 (26) :6206-6212
[6]   Residue-based control of helix shape in beta-peptide oligomers [J].
Appella, DH ;
Christianson, LA ;
Klein, DA ;
Powell, DR ;
Huang, XL ;
Barchi, JJ ;
Gellman, SH .
NATURE, 1997, 387 (6631) :381-384
[7]   Formation of short, stable helices in aqueous solution by β-amino acid hexamers [J].
Appella, DH ;
Barchi, JJ ;
Durell, SR ;
Gellman, SH .
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 1999, 121 (10) :2309-2310
[8]   beta-peptide foldamers: Robust Helix formation in a new family of beta-amino acid oligomers [J].
Appella, DH ;
Christianson, LA ;
Karle, IL ;
Powell, DR ;
Gellman, SH .
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 1996, 118 (51) :13071-13072
[9]   NMR determination of the major solution conformation of a peptoid pentamer with chiral side chains [J].
Armand, P ;
Kirshenbaum, K ;
Goldsmith, RA ;
Farr-Jones, S ;
Barron, AE ;
Truong, KTV ;
Dill, KA ;
Mierke, DF ;
Cohen, FE ;
Zuckermann, RN ;
Bradley, EK .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1998, 95 (08) :4309-4314
[10]   Designed self-generation of an extended helical structure from an achiral polyheterocyclic strand [J].
Bassani, DM ;
Lehn, JM ;
Baum, G ;
Fenske, D .
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION IN ENGLISH, 1997, 36 (17) :1845-1847