Lyotropic liquid crystals formed from ACHC-Rich β-peptides

William C. Pomerantz, Virany M. Yuwono, Ryan Drake, Jeffrey D. Hartgerink, Nicholas L. Abbott, Samuel H. Gellman

Research output: Contribution to journalArticle

37 Citations (Scopus)

Abstract

We have examined the effect of β-peptide modifications on the propensity of these helical molecules to form lyotropic liquid crystalline (LC) phases in water. All of the β-peptides we have examined contain 10 residues. In each case, at least three residues are derived from trans-2-aminocyclohexanecarboxylic acid (ACHC), which strongly promotes folding to a 14-helical conformation. The structural features varied include the number of ACHC residues, the nature and spatial arrangement of charged side chains (cationic vs anionic), and the identity of groups at the β-peptide termini. We found that relatively small changes (e.g., swapping the positions of a cationic and an anionic side chain) could have large effects, such as abrogation of LC phase formation. The trends revealed by sequence-property studies led to the design of LC-forming β-peptides that bear biomolecular recognition groups (biotin or the tripeptide Arg-Gly-Asp). Structural analysis via circular dichroism and cryo-transmission electron microscopy revealed the existence of two different types of self-associated species, globular aggregates and nanofibers. Nanofibers are the predominant assembly formed at concentrations that lead to LC phase formation, and we conclude that these nanofibers are the functional mesogens. Overall, these studies show how the modularity of β-peptide oligomers enables elucidation of the relationship between molecular structure and large-scale self-assembly behavior.

Original languageEnglish (US)
Pages (from-to)13604-13613
Number of pages10
JournalJournal of the American Chemical Society
Volume133
Issue number34
DOIs
StatePublished - Aug 31 2011

Fingerprint

Liquid Crystals
Liquid crystals
Peptides
Nanofibers
Acids
Crystalline materials
Liquids
Cryoelectron Microscopy
Dichroism
Biotin
Circular Dichroism
Molecular Structure
Transmission Electron Microscopy
Oligomers
Structural analysis
Self assembly
Molecular structure
Conformations
2-aminocyclohexanecarboxylic acid
Transmission electron microscopy

Cite this

Pomerantz, W. C., Yuwono, V. M., Drake, R., Hartgerink, J. D., Abbott, N. L., & Gellman, S. H. (2011). Lyotropic liquid crystals formed from ACHC-Rich β-peptides. Journal of the American Chemical Society, 133(34), 13604-13613. https://doi.org/10.1021/ja204874h

Lyotropic liquid crystals formed from ACHC-Rich β-peptides. / Pomerantz, William C.; Yuwono, Virany M.; Drake, Ryan; Hartgerink, Jeffrey D.; Abbott, Nicholas L.; Gellman, Samuel H.

In: Journal of the American Chemical Society, Vol. 133, No. 34, 31.08.2011, p. 13604-13613.

Research output: Contribution to journalArticle

Pomerantz, WC, Yuwono, VM, Drake, R, Hartgerink, JD, Abbott, NL & Gellman, SH 2011, 'Lyotropic liquid crystals formed from ACHC-Rich β-peptides', Journal of the American Chemical Society, vol. 133, no. 34, pp. 13604-13613. https://doi.org/10.1021/ja204874h
Pomerantz WC, Yuwono VM, Drake R, Hartgerink JD, Abbott NL, Gellman SH. Lyotropic liquid crystals formed from ACHC-Rich β-peptides. Journal of the American Chemical Society. 2011 Aug 31;133(34):13604-13613. https://doi.org/10.1021/ja204874h
Pomerantz, William C. ; Yuwono, Virany M. ; Drake, Ryan ; Hartgerink, Jeffrey D. ; Abbott, Nicholas L. ; Gellman, Samuel H. / Lyotropic liquid crystals formed from ACHC-Rich β-peptides. In: Journal of the American Chemical Society. 2011 ; Vol. 133, No. 34. pp. 13604-13613.
@article{6e59c2583ea349c39bd22833a660da88,
title = "Lyotropic liquid crystals formed from ACHC-Rich β-peptides",
abstract = "We have examined the effect of β-peptide modifications on the propensity of these helical molecules to form lyotropic liquid crystalline (LC) phases in water. All of the β-peptides we have examined contain 10 residues. In each case, at least three residues are derived from trans-2-aminocyclohexanecarboxylic acid (ACHC), which strongly promotes folding to a 14-helical conformation. The structural features varied include the number of ACHC residues, the nature and spatial arrangement of charged side chains (cationic vs anionic), and the identity of groups at the β-peptide termini. We found that relatively small changes (e.g., swapping the positions of a cationic and an anionic side chain) could have large effects, such as abrogation of LC phase formation. The trends revealed by sequence-property studies led to the design of LC-forming β-peptides that bear biomolecular recognition groups (biotin or the tripeptide Arg-Gly-Asp). Structural analysis via circular dichroism and cryo-transmission electron microscopy revealed the existence of two different types of self-associated species, globular aggregates and nanofibers. Nanofibers are the predominant assembly formed at concentrations that lead to LC phase formation, and we conclude that these nanofibers are the functional mesogens. Overall, these studies show how the modularity of β-peptide oligomers enables elucidation of the relationship between molecular structure and large-scale self-assembly behavior.",
author = "Pomerantz, {William C.} and Yuwono, {Virany M.} and Ryan Drake and Hartgerink, {Jeffrey D.} and Abbott, {Nicholas L.} and Gellman, {Samuel H.}",
year = "2011",
month = "8",
day = "31",
doi = "10.1021/ja204874h",
language = "English (US)",
volume = "133",
pages = "13604--13613",
journal = "Journal of the American Chemical Society",
issn = "0002-7863",
publisher = "American Chemical Society",
number = "34",

}

TY - JOUR

T1 - Lyotropic liquid crystals formed from ACHC-Rich β-peptides

AU - Pomerantz, William C.

AU - Yuwono, Virany M.

AU - Drake, Ryan

AU - Hartgerink, Jeffrey D.

AU - Abbott, Nicholas L.

AU - Gellman, Samuel H.

PY - 2011/8/31

Y1 - 2011/8/31

N2 - We have examined the effect of β-peptide modifications on the propensity of these helical molecules to form lyotropic liquid crystalline (LC) phases in water. All of the β-peptides we have examined contain 10 residues. In each case, at least three residues are derived from trans-2-aminocyclohexanecarboxylic acid (ACHC), which strongly promotes folding to a 14-helical conformation. The structural features varied include the number of ACHC residues, the nature and spatial arrangement of charged side chains (cationic vs anionic), and the identity of groups at the β-peptide termini. We found that relatively small changes (e.g., swapping the positions of a cationic and an anionic side chain) could have large effects, such as abrogation of LC phase formation. The trends revealed by sequence-property studies led to the design of LC-forming β-peptides that bear biomolecular recognition groups (biotin or the tripeptide Arg-Gly-Asp). Structural analysis via circular dichroism and cryo-transmission electron microscopy revealed the existence of two different types of self-associated species, globular aggregates and nanofibers. Nanofibers are the predominant assembly formed at concentrations that lead to LC phase formation, and we conclude that these nanofibers are the functional mesogens. Overall, these studies show how the modularity of β-peptide oligomers enables elucidation of the relationship between molecular structure and large-scale self-assembly behavior.

AB - We have examined the effect of β-peptide modifications on the propensity of these helical molecules to form lyotropic liquid crystalline (LC) phases in water. All of the β-peptides we have examined contain 10 residues. In each case, at least three residues are derived from trans-2-aminocyclohexanecarboxylic acid (ACHC), which strongly promotes folding to a 14-helical conformation. The structural features varied include the number of ACHC residues, the nature and spatial arrangement of charged side chains (cationic vs anionic), and the identity of groups at the β-peptide termini. We found that relatively small changes (e.g., swapping the positions of a cationic and an anionic side chain) could have large effects, such as abrogation of LC phase formation. The trends revealed by sequence-property studies led to the design of LC-forming β-peptides that bear biomolecular recognition groups (biotin or the tripeptide Arg-Gly-Asp). Structural analysis via circular dichroism and cryo-transmission electron microscopy revealed the existence of two different types of self-associated species, globular aggregates and nanofibers. Nanofibers are the predominant assembly formed at concentrations that lead to LC phase formation, and we conclude that these nanofibers are the functional mesogens. Overall, these studies show how the modularity of β-peptide oligomers enables elucidation of the relationship between molecular structure and large-scale self-assembly behavior.

UR - http://www.scopus.com/inward/record.url?scp=80052094249&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=80052094249&partnerID=8YFLogxK

U2 - 10.1021/ja204874h

DO - 10.1021/ja204874h

M3 - Article

C2 - 21815636

AN - SCOPUS:80052094249

VL - 133

SP - 13604

EP - 13613

JO - Journal of the American Chemical Society

JF - Journal of the American Chemical Society

SN - 0002-7863

IS - 34

ER -