Cryo electron tomography reveals confined complex morphologies of tripeptide-containing amphiphilic double-comb diblock copolymers

A.L. Parry; P.H.H. Bomans; S.J. Holder; N.A.J.M. Sommerdijk; S.C.G. Biagini

doi:10.1002/anie.200802834

Cryo electron tomography reveals confined complex morphologies of tripeptide-containing amphiphilic double-comb diblock copolymers

A.L. Parry, P.H.H. Bomans, S.J. Holder, N.A.J.M. Sommerdijk, S.C.G. Biagini

Materials and Interface Chemistry

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

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Abstract

(Chemical Equation Presented) Sequence sets structure: Amphiphilic norbornene-based double-comb diblock polymers with peptide and oligo(ethylene oxide) side chains aggregate in water to form unprecedented complex morphologies depending on the amino acid sequence of the peptide. The internal structures of the aggregates observed by cryo electron tomography show densely folded and highly branched wormlike micelles (left) and spherical aggregates with a bicontinuous architecture (right). © 2008 Wiley-VCH Verlag GmbH & Co. KGaA.

Original language	English
Pages (from-to)	8859-8862
Journal	Angewandte Chemie - International Edition
Volume	47
Issue number	46
DOIs	https://doi.org/10.1002/anie.200802834
Publication status	Published - 2008

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10.1002/anie.200802834

Center for Multiscale Electron Microscopy (CMEM)
Heiner Friedrich (Manager), Rick Joosten (Education/research officer), Pauline Schmit (Education/research officer), Ingeborg Schreur - Piet (Other) & Anne Spoelstra (Education/research officer)
Physical Chemistry
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abstract = "(Chemical Equation Presented) Sequence sets structure: Amphiphilic norbornene-based double-comb diblock polymers with peptide and oligo(ethylene oxide) side chains aggregate in water to form unprecedented complex morphologies depending on the amino acid sequence of the peptide. The internal structures of the aggregates observed by cryo electron tomography show densely folded and highly branched wormlike micelles (left) and spherical aggregates with a bicontinuous architecture (right). {\textcopyright} 2008 Wiley-VCH Verlag GmbH & Co. KGaA.",

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AU - Parry, A.L.

AU - Bomans, P.H.H.

AU - Holder, S.J.

AU - Sommerdijk, N.A.J.M.

AU - Biagini, S.C.G.

PY - 2008

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N2 - (Chemical Equation Presented) Sequence sets structure: Amphiphilic norbornene-based double-comb diblock polymers with peptide and oligo(ethylene oxide) side chains aggregate in water to form unprecedented complex morphologies depending on the amino acid sequence of the peptide. The internal structures of the aggregates observed by cryo electron tomography show densely folded and highly branched wormlike micelles (left) and spherical aggregates with a bicontinuous architecture (right). © 2008 Wiley-VCH Verlag GmbH & Co. KGaA.

AB - (Chemical Equation Presented) Sequence sets structure: Amphiphilic norbornene-based double-comb diblock polymers with peptide and oligo(ethylene oxide) side chains aggregate in water to form unprecedented complex morphologies depending on the amino acid sequence of the peptide. The internal structures of the aggregates observed by cryo electron tomography show densely folded and highly branched wormlike micelles (left) and spherical aggregates with a bicontinuous architecture (right). © 2008 Wiley-VCH Verlag GmbH & Co. KGaA.

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DO - 10.1002/anie.200802834

M3 - Article

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Cryo electron tomography reveals confined complex morphologies of tripeptide-containing amphiphilic double-comb diblock copolymers

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