Crystalline cyclic peptide nanotubes at interfaces

Hanna Rapaport; Hui Sun Kim; Kristian Kjaer; Paul B. Howes; Sidney Cohen; Jens Als-Nielsen; M. Reza Ghadiri; Leslie Leiserowitz; Meir Lahav

doi:10.1021/ja982420i

Crystalline cyclic peptide nanotubes at interfaces

Hanna Rapaport, Hui Sun Kim, Kristian Kjaer, Paul B. Howes, Sidney Cohen, Jens Als-Nielsen, M. Reza Ghadiri, Leslie Leiserowitz, Meir Lahav

Research output: Contribution to journal › Article › peer-review

46 Scopus citations

Abstract

The assembly, orientation, and structural features of nanoscale tubes composed of cyclic peptides, formed at the air-water interface, were detected by grazing incidence X-ray diffraction (GIXD). The peptide cyclo-[(L-Phe-D- N-MeAla-)₄] (1) exhibits two-dimensional crystallinity in which the plane of the peptide ring is parallel to the water interface. The peptide cyclo-[(L- Trp-D-Leu)₃-L-Ser-D-Leu] (2) forms predominantly planar aggregates composed of several tubes, lying with their long axes parallel to the air-water interface. In contrast, the peptide cyclo-[(L-Trp-D-Leu)₄] (3) exhibits a very low tendency to form ordered two-dimensional arrays of nanotubes. Films of peptides 2 and 3 as well as their mixtures with the phospholipid DPPA were transferred onto a solid support and visualized by scanning force microscopy (SFM).

Original language	English
Pages (from-to)	1186-1191
Number of pages	6
Journal	Journal of the American Chemical Society
Volume	121
Issue number	6
DOIs	https://doi.org/10.1021/ja982420i
State	Published - 17 Feb 1999
Externally published	Yes

ASJC Scopus subject areas

Catalysis
General Chemistry
Biochemistry
Colloid and Surface Chemistry

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10.1021/ja982420i

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@article{025b3a6a9ed04dd6a2f0505b42e7f3c7,

title = "Crystalline cyclic peptide nanotubes at interfaces",

abstract = "The assembly, orientation, and structural features of nanoscale tubes composed of cyclic peptides, formed at the air-water interface, were detected by grazing incidence X-ray diffraction (GIXD). The peptide cyclo-[(L-Phe-D- N-MeAla-)4] (1) exhibits two-dimensional crystallinity in which the plane of the peptide ring is parallel to the water interface. The peptide cyclo-[(L- Trp-D-Leu)3-L-Ser-D-Leu] (2) forms predominantly planar aggregates composed of several tubes, lying with their long axes parallel to the air-water interface. In contrast, the peptide cyclo-[(L-Trp-D-Leu)4] (3) exhibits a very low tendency to form ordered two-dimensional arrays of nanotubes. Films of peptides 2 and 3 as well as their mixtures with the phospholipid DPPA were transferred onto a solid support and visualized by scanning force microscopy (SFM).",

author = "Hanna Rapaport and Kim, \{Hui Sun\} and Kristian Kjaer and Howes, \{Paul B.\} and Sidney Cohen and Jens Als-Nielsen and \{Reza Ghadiri\}, M. and Leslie Leiserowitz and Meir Lahav",

year = "1999",

month = feb,

day = "17",

doi = "10.1021/ja982420i",

language = "English",

volume = "121",

pages = "1186--1191",

journal = "Journal of the American Chemical Society",

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publisher = "American Chemical Society",

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TY - JOUR

T1 - Crystalline cyclic peptide nanotubes at interfaces

AU - Rapaport, Hanna

AU - Kim, Hui Sun

AU - Kjaer, Kristian

AU - Howes, Paul B.

AU - Cohen, Sidney

AU - Als-Nielsen, Jens

AU - Reza Ghadiri, M.

AU - Leiserowitz, Leslie

AU - Lahav, Meir

PY - 1999/2/17

Y1 - 1999/2/17

N2 - The assembly, orientation, and structural features of nanoscale tubes composed of cyclic peptides, formed at the air-water interface, were detected by grazing incidence X-ray diffraction (GIXD). The peptide cyclo-[(L-Phe-D- N-MeAla-)4] (1) exhibits two-dimensional crystallinity in which the plane of the peptide ring is parallel to the water interface. The peptide cyclo-[(L- Trp-D-Leu)3-L-Ser-D-Leu] (2) forms predominantly planar aggregates composed of several tubes, lying with their long axes parallel to the air-water interface. In contrast, the peptide cyclo-[(L-Trp-D-Leu)4] (3) exhibits a very low tendency to form ordered two-dimensional arrays of nanotubes. Films of peptides 2 and 3 as well as their mixtures with the phospholipid DPPA were transferred onto a solid support and visualized by scanning force microscopy (SFM).

AB - The assembly, orientation, and structural features of nanoscale tubes composed of cyclic peptides, formed at the air-water interface, were detected by grazing incidence X-ray diffraction (GIXD). The peptide cyclo-[(L-Phe-D- N-MeAla-)4] (1) exhibits two-dimensional crystallinity in which the plane of the peptide ring is parallel to the water interface. The peptide cyclo-[(L- Trp-D-Leu)3-L-Ser-D-Leu] (2) forms predominantly planar aggregates composed of several tubes, lying with their long axes parallel to the air-water interface. In contrast, the peptide cyclo-[(L-Trp-D-Leu)4] (3) exhibits a very low tendency to form ordered two-dimensional arrays of nanotubes. Films of peptides 2 and 3 as well as their mixtures with the phospholipid DPPA were transferred onto a solid support and visualized by scanning force microscopy (SFM).

UR - https://www.scopus.com/pages/publications/0345320328

U2 - 10.1021/ja982420i

DO - 10.1021/ja982420i

M3 - Article

AN - SCOPUS:0345320328

SN - 0002-7863

VL - 121

SP - 1186

EP - 1191

JO - Journal of the American Chemical Society

JF - Journal of the American Chemical Society

IS - 6

ER -

Crystalline cyclic peptide nanotubes at interfaces

Abstract

ASJC Scopus subject areas

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