Remodeling cross-β nanotube surfaces with peptide/lipid chimeras

Rong Ni; W. Seth Childers; Kenneth I. Hardcastle; Anil K. Mehta; David G. Lynn

doi:10.1002/anie.201201173

Remodeling cross-β nanotube surfaces with peptide/lipid chimeras

Rong Ni, W. Seth Childers, Kenneth I. Hardcastle, Anil K. Mehta^*, David G. Lynn

^*Corresponding author for this work

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

37 Citations (Scopus)

Abstract

Between the sheets: A unique cross-β-peptide amphiphile assembly positions the acyl chain within the hydrophobic cross-β laminate (see picture; acyl chain: red, peptide: gray, lysine: blue). The atomic-level structure of the self-assembled surface can also be systematically altered, opening the possibility to create a wide range of nanostructured biomaterials.

Original language	English
Pages (from-to)	6635-6638
Number of pages	4
Journal	Angewandte Chemie - International Edition
Volume	51
Issue number	27
DOIs	https://doi.org/10.1002/anie.201201173
Publication status	Published - 2 Jul 2012
Externally published	Yes

Keywords

NMR spectroscopy
amphiphiles
nanotubes
peptides
self-assembly

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10.1002/anie.201201173

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title = "Remodeling cross-β nanotube surfaces with peptide/lipid chimeras",

abstract = "Between the sheets: A unique cross-β-peptide amphiphile assembly positions the acyl chain within the hydrophobic cross-β laminate (see picture; acyl chain: red, peptide: gray, lysine: blue). The atomic-level structure of the self-assembled surface can also be systematically altered, opening the possibility to create a wide range of nanostructured biomaterials.",

keywords = "NMR spectroscopy, amphiphiles, nanotubes, peptides, self-assembly",

author = "Rong Ni and Childers, \{W. Seth\} and Hardcastle, \{Kenneth I.\} and Mehta, \{Anil K.\} and Lynn, \{David G.\}",

year = "2012",

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T1 - Remodeling cross-β nanotube surfaces with peptide/lipid chimeras

AU - Ni, Rong

AU - Childers, W. Seth

AU - Hardcastle, Kenneth I.

AU - Mehta, Anil K.

AU - Lynn, David G.

PY - 2012/7/2

Y1 - 2012/7/2

N2 - Between the sheets: A unique cross-β-peptide amphiphile assembly positions the acyl chain within the hydrophobic cross-β laminate (see picture; acyl chain: red, peptide: gray, lysine: blue). The atomic-level structure of the self-assembled surface can also be systematically altered, opening the possibility to create a wide range of nanostructured biomaterials.

AB - Between the sheets: A unique cross-β-peptide amphiphile assembly positions the acyl chain within the hydrophobic cross-β laminate (see picture; acyl chain: red, peptide: gray, lysine: blue). The atomic-level structure of the self-assembled surface can also be systematically altered, opening the possibility to create a wide range of nanostructured biomaterials.

KW - NMR spectroscopy

KW - amphiphiles

KW - nanotubes

KW - peptides

KW - self-assembly

UR - https://www.webofscience.com/wos/woscc/full-record/WOS:000305987900015

UR - https://openalex.org/W2048649981

UR - https://www.scopus.com/pages/publications/84863226677

U2 - 10.1002/anie.201201173

DO - 10.1002/anie.201201173

M3 - Journal Article

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JO - Angewandte Chemie - International Edition

JF - Angewandte Chemie - International Edition

IS - 27

ER -

Remodeling cross-β nanotube surfaces with peptide/lipid chimeras

Abstract

Keywords

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