Publication

Chain length dependence of the helix orientation in Langmuir-Blodgett monolayers of alpha-helical diblock copolypeptides

Nguyen, L-T. T., Ardana, A., Vorenkamp, E. J., ten Brinke, G. & Schouten, A. J., 2010, In : Soft Matter. 6, 12, p. 2774-2785 12 p.

Research output: Contribution to journalArticleAcademicpeer-review

APA

Nguyen, L-T. T., Ardana, A., Vorenkamp, E. J., ten Brinke, G., & Schouten, A. J. (2010). Chain length dependence of the helix orientation in Langmuir-Blodgett monolayers of alpha-helical diblock copolypeptides. Soft Matter, 6(12), 2774-2785. https://doi.org/10.1039/c001163k

Author

Nguyen, Le-Thu T. ; Ardana, Aditya ; Vorenkamp, Eltjo J. ; ten Brinke, Gerrit ; Schouten, Arend J. / Chain length dependence of the helix orientation in Langmuir-Blodgett monolayers of alpha-helical diblock copolypeptides. In: Soft Matter. 2010 ; Vol. 6, No. 12. pp. 2774-2785.

Harvard

Nguyen, L-TT, Ardana, A, Vorenkamp, EJ, ten Brinke, G & Schouten, AJ 2010, 'Chain length dependence of the helix orientation in Langmuir-Blodgett monolayers of alpha-helical diblock copolypeptides', Soft Matter, vol. 6, no. 12, pp. 2774-2785. https://doi.org/10.1039/c001163k

Standard

Chain length dependence of the helix orientation in Langmuir-Blodgett monolayers of alpha-helical diblock copolypeptides. / Nguyen, Le-Thu T.; Ardana, Aditya; Vorenkamp, Eltjo J.; ten Brinke, Gerrit; Schouten, Arend J.

In: Soft Matter, Vol. 6, No. 12, 2010, p. 2774-2785.

Research output: Contribution to journalArticleAcademicpeer-review

Vancouver

Nguyen L-TT, Ardana A, Vorenkamp EJ, ten Brinke G, Schouten AJ. Chain length dependence of the helix orientation in Langmuir-Blodgett monolayers of alpha-helical diblock copolypeptides. Soft Matter. 2010;6(12):2774-2785. https://doi.org/10.1039/c001163k


BibTeX

@article{c5ecce1574e8437492e08e073792736c,
title = "Chain length dependence of the helix orientation in Langmuir-Blodgett monolayers of alpha-helical diblock copolypeptides",
abstract = "The effect of chain length on the helix orientation of alpha-helical diblock copolypeptides in Langmuir and Langmuir-Blodgett monolayers is reported for the first time. Amphiphilic diblock copolypeptides (PLGA-b-PMLGSLGs) of poly(alpha-L-glutamic acid) (PLGA) and poly(gamma-methyl-L-glutamate-ran-gamma-stearyl-L-glutamate) with 30 mol{\%} of stearyl substituents (PMLGSLG) of various block lengths were studied. The tilt angle between the helices and the substrate-normal decreases upon increasing the transfer pressure coincident with {"}double brush{"} formation. The hydrophobic block length strongly affects the maximum surface chain density and thereby the helix orientation of the diblock copolypeptides. Increasing the degree of polymerization of the hydrophobic block (DP(PMLGSLG)) results in an increase in the helix tilt angle tentatively attributed to the off-axis interactions of the unscreened peptide dipoles between the parallel aligned alpha-helices. In those cases where the alkyl side chains surround the PMLGSLG helices, the smallest helix tilt angle of 29 degrees for the PMLGSLG block and 67 degrees for the PLGA block were obtained for the diblock copolymer of DP(PLGA) 37 and DP(PMLGSLG) 24. For smaller DP values of the hydrophobic block, in particular the diblock copolymer having DP(PMLGSLG) 11, the long alkyl side chains are partially expelled from the brush layer and the alpha-helices of the PMLGSLG block are oriented nearly perpendicular to the interface.",
keywords = "AIR-WATER-INTERFACE, SELF-ASSEMBLED MONOLAYERS, X-RAY REFLECTOMETRY, MOLECULAR-ORIENTATION, POLYMER BRUSHES, POLY(L-GLUTAMIC ACID), AIR/WATER INTERFACE, INFRARED-SPECTRA, COIL TRANSITION, POLYPEPTIDES",
author = "Nguyen, {Le-Thu T.} and Aditya Ardana and Vorenkamp, {Eltjo J.} and {ten Brinke}, Gerrit and Schouten, {Arend J.}",
year = "2010",
doi = "10.1039/c001163k",
language = "English",
volume = "6",
pages = "2774--2785",
journal = "Soft Matter",
issn = "1744-683X",
publisher = "ROYAL SOC CHEMISTRY",
number = "12",

}

RIS

TY - JOUR

T1 - Chain length dependence of the helix orientation in Langmuir-Blodgett monolayers of alpha-helical diblock copolypeptides

AU - Nguyen, Le-Thu T.

AU - Ardana, Aditya

AU - Vorenkamp, Eltjo J.

AU - ten Brinke, Gerrit

AU - Schouten, Arend J.

PY - 2010

Y1 - 2010

N2 - The effect of chain length on the helix orientation of alpha-helical diblock copolypeptides in Langmuir and Langmuir-Blodgett monolayers is reported for the first time. Amphiphilic diblock copolypeptides (PLGA-b-PMLGSLGs) of poly(alpha-L-glutamic acid) (PLGA) and poly(gamma-methyl-L-glutamate-ran-gamma-stearyl-L-glutamate) with 30 mol% of stearyl substituents (PMLGSLG) of various block lengths were studied. The tilt angle between the helices and the substrate-normal decreases upon increasing the transfer pressure coincident with "double brush" formation. The hydrophobic block length strongly affects the maximum surface chain density and thereby the helix orientation of the diblock copolypeptides. Increasing the degree of polymerization of the hydrophobic block (DP(PMLGSLG)) results in an increase in the helix tilt angle tentatively attributed to the off-axis interactions of the unscreened peptide dipoles between the parallel aligned alpha-helices. In those cases where the alkyl side chains surround the PMLGSLG helices, the smallest helix tilt angle of 29 degrees for the PMLGSLG block and 67 degrees for the PLGA block were obtained for the diblock copolymer of DP(PLGA) 37 and DP(PMLGSLG) 24. For smaller DP values of the hydrophobic block, in particular the diblock copolymer having DP(PMLGSLG) 11, the long alkyl side chains are partially expelled from the brush layer and the alpha-helices of the PMLGSLG block are oriented nearly perpendicular to the interface.

AB - The effect of chain length on the helix orientation of alpha-helical diblock copolypeptides in Langmuir and Langmuir-Blodgett monolayers is reported for the first time. Amphiphilic diblock copolypeptides (PLGA-b-PMLGSLGs) of poly(alpha-L-glutamic acid) (PLGA) and poly(gamma-methyl-L-glutamate-ran-gamma-stearyl-L-glutamate) with 30 mol% of stearyl substituents (PMLGSLG) of various block lengths were studied. The tilt angle between the helices and the substrate-normal decreases upon increasing the transfer pressure coincident with "double brush" formation. The hydrophobic block length strongly affects the maximum surface chain density and thereby the helix orientation of the diblock copolypeptides. Increasing the degree of polymerization of the hydrophobic block (DP(PMLGSLG)) results in an increase in the helix tilt angle tentatively attributed to the off-axis interactions of the unscreened peptide dipoles between the parallel aligned alpha-helices. In those cases where the alkyl side chains surround the PMLGSLG helices, the smallest helix tilt angle of 29 degrees for the PMLGSLG block and 67 degrees for the PLGA block were obtained for the diblock copolymer of DP(PLGA) 37 and DP(PMLGSLG) 24. For smaller DP values of the hydrophobic block, in particular the diblock copolymer having DP(PMLGSLG) 11, the long alkyl side chains are partially expelled from the brush layer and the alpha-helices of the PMLGSLG block are oriented nearly perpendicular to the interface.

KW - AIR-WATER-INTERFACE

KW - SELF-ASSEMBLED MONOLAYERS

KW - X-RAY REFLECTOMETRY

KW - MOLECULAR-ORIENTATION

KW - POLYMER BRUSHES

KW - POLY(L-GLUTAMIC ACID)

KW - AIR/WATER INTERFACE

KW - INFRARED-SPECTRA

KW - COIL TRANSITION

KW - POLYPEPTIDES

U2 - 10.1039/c001163k

DO - 10.1039/c001163k

M3 - Article

VL - 6

SP - 2774

EP - 2785

JO - Soft Matter

JF - Soft Matter

SN - 1744-683X

IS - 12

ER -

ID: 5101088