Insights into the Molecular Architecture of a Peptide Nanotube Using FTIR and Solid-State NMR Spectroscopic Measurements on an Aligned Sample

被引：51

作者：

Middleton, David A. ^{[1
]}

Madine, Jillian ^{[1
]}

Castelletto, Valeria ^{[2
]}

Hamley, Ian W. ^{[2
]}

机构：

[1] Univ Liverpool, Inst Integrat Biol, Liverpool L69 7ZB, Merseyside, England

[2] Univ Reading, Dept Chem, Reading RG6 6AD, Berks, England

来源：

ANGEWANDTE CHEMIE-INTERNATIONAL EDITION | 2013年 / 52卷 / 40期

基金：

英国工程与自然科学研究理事会;

关键词：

IR spectroscopy; nanotubes; NMR spectroscopy; peptides; AMIDE-I; POLYPEPTIDES; PROTEIN;

D O I：

10.1002/anie.201301960

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

Queuing up: Molecular orientation within macroscopically aligned nanotubes of the peptide AAAAAAK can be studied by solid-state NMR and IR spectroscopy. Line shape analysis of the NMR spectra indicates that the peptide N-H bonds are tilted 65-70° relative to the nanotube long axis. Re-evaluation of earlier X-ray fiber diffraction data suggests that the peptide molecules are hydrogen-bonded in a helical arrangement along the nanotube axis. Copyright © 2013 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.

引用

页码：10537 / 10540

页数：4

共 30 条

[1] In vitro self-assembly from a simple protein of tailorable nanotubes building block [J].

Ballister, Edward R. ;

Lai, Angela H. ;

Zuckermann, Ronald N. ;

Cheng, Yifan ;

Mougous, Joseph D. .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2008, 105 (10) :3733-3738

[2] The structural and topological analysis of membrane-associated polypeptides by oriented solid-state NMR spectroscopy: Established concepts and novel developments [J].

Bechinger, Burkhard ;

Resende, Jarbas M. ;

Aisenbrey, Christopher .

BIOPHYSICAL CHEMISTRY, 2011, 153 (2-3) :115-125

[3] 13C isotope labeling of hydrophobic peptides.: Origin of the anomalous intensity distribution in the infrared amide I spectral region of β-sheet structures [J].

Brauner, JW ;

Dugan, C ;

Mendelsohn, R .

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 2000, 122 (04) :677-683

[4] Peptide Nanotube Nematic Phase [J].

Bucak, S. ;

Cenker, C. ;

Nasir, I. ;

Olsson, U. ;

Zackrisson, M. .

LANGMUIR, 2009, 25 (08) :4262-4265

[5] Influence of the Solvent on the Self-Assembly of a Modified Amyloid Beta Peptide Fragment. I. Morphological Investigation [J].

Castelletto, V. ;

Hamley, I. W. ;

Harris, P. J. F. ;

Olsson, U. ;

Spencer, N. .

JOURNAL OF PHYSICAL CHEMISTRY B, 2009, 113 (29) :9978-9987

[6] Structure of single-wall peptide nanotubes: in situ flow aligning X-ray diffraction [J].

Castelletto, Valeria ;

Nutt, David R. ;

Hamley, Ian W. ;

Bucak, Seyda ;

Cenker, Celen ;

Olsson, Ulf .

CHEMICAL COMMUNICATIONS, 2010, 46 (34) :6270-6272

[7]

Cherny I., 2008, Angew. Chem, V120, P4128

[8] Amyloids: Not only pathological agents but also ordered nanomaterials [J].

Cherny, Izhack ;

Gazit, Ehud .

ANGEWANDTE CHEMIE-INTERNATIONAL EDITION, 2008, 47 (22) :4062-4069

[9]

Childers W. S., 2010, ANGEW CHEM-GER EDIT, V122, P4198, DOI [10.1002/ange.201000212, DOI 10.1002/ANGE.201000212]

[10] Peptides Organized as Bilayer Membranes [J].

Childers, W. Seth ;

Mehta, Anil K. ;

Ni, Rong ;

Taylor, Jeannette V. ;

Lynn, David G. .

ANGEWANDTE CHEMIE-INTERNATIONAL EDITION, 2010, 49 (24) :4104-4107

← 1 2 3 →