Nanodomain-induced chain folding in poly(γ-benzyl-L-glutamate)-b-polyglycine diblock copolymers

P. Papadopoulos; G. Floudas; I. Schnell; T. Aliferis; H. Iatrou; N. Hadjichristidis

doi:10.1021/bm0501860

Nanodomain-induced chain folding in poly(γ-benzyl-L-glutamate)-b-polyglycine diblock copolymers

P. Papadopoulos, G. Floudas^*, I. Schnell, T. Aliferis, H. Iatrou, N. Hadjichristidis

^*Corresponding author for this work

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

62 Scopus citations

Abstract

We report on the self-assembly mechanism and dynamics in a series of poly(γ-benzyl-L-glutamate)-b-poly(glycine) (PBLG-b-PGly) diblock copolymers within the composition range 0.67 ≤ f_PBLG ≤ 0.97 and the temperature (T) range 303 < T < 433 K. Small- and wide-angle X-ray scattering, ¹³C NMR, and differential scanning calorimetry are used for the structure investigation coupled with dielectric spectroscopy for both the peptide secondary structure and the associated dynamics. These techniques provide not only the nanophase morphology but also the type and persistence of peptide secondary structures. The thermodynamic confinement of the blocks within the nanodomains and the disparity in their packing efficiency results in multiple chain folding of the PGly secondary structure that effectively stabilize a lamellar morphology for high f_PBLG. Nanoscale confinement proves to be important in controlling the persistence length of secondary peptide motifs.

Original language	English (US)
Pages (from-to)	2352-2361
Number of pages	10
Journal	Biomacromolecules
Volume	6
Issue number	4
DOIs	https://doi.org/10.1021/bm0501860
State	Published - Jul 2005
Externally published	Yes

ASJC Scopus subject areas

Bioengineering
Biomaterials
Polymers and Plastics
Materials Chemistry

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10.1021/bm0501860

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title = "Nanodomain-induced chain folding in poly(γ-benzyl-L-glutamate)-b-polyglycine diblock copolymers",

abstract = "We report on the self-assembly mechanism and dynamics in a series of poly(γ-benzyl-L-glutamate)-b-poly(glycine) (PBLG-b-PGly) diblock copolymers within the composition range 0.67 ≤ fPBLG ≤ 0.97 and the temperature (T) range 303 < T < 433 K. Small- and wide-angle X-ray scattering, 13C NMR, and differential scanning calorimetry are used for the structure investigation coupled with dielectric spectroscopy for both the peptide secondary structure and the associated dynamics. These techniques provide not only the nanophase morphology but also the type and persistence of peptide secondary structures. The thermodynamic confinement of the blocks within the nanodomains and the disparity in their packing efficiency results in multiple chain folding of the PGly secondary structure that effectively stabilize a lamellar morphology for high fPBLG. Nanoscale confinement proves to be important in controlling the persistence length of secondary peptide motifs.",

author = "P. Papadopoulos and G. Floudas and I. Schnell and T. Aliferis and H. Iatrou and N. Hadjichristidis",

year = "2005",

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language = "English (US)",

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T1 - Nanodomain-induced chain folding in poly(γ-benzyl-L-glutamate)-b-polyglycine diblock copolymers

AU - Papadopoulos, P.

AU - Floudas, G.

AU - Schnell, I.

AU - Aliferis, T.

AU - Iatrou, H.

AU - Hadjichristidis, N.

PY - 2005/7

Y1 - 2005/7

N2 - We report on the self-assembly mechanism and dynamics in a series of poly(γ-benzyl-L-glutamate)-b-poly(glycine) (PBLG-b-PGly) diblock copolymers within the composition range 0.67 ≤ fPBLG ≤ 0.97 and the temperature (T) range 303 < T < 433 K. Small- and wide-angle X-ray scattering, 13C NMR, and differential scanning calorimetry are used for the structure investigation coupled with dielectric spectroscopy for both the peptide secondary structure and the associated dynamics. These techniques provide not only the nanophase morphology but also the type and persistence of peptide secondary structures. The thermodynamic confinement of the blocks within the nanodomains and the disparity in their packing efficiency results in multiple chain folding of the PGly secondary structure that effectively stabilize a lamellar morphology for high fPBLG. Nanoscale confinement proves to be important in controlling the persistence length of secondary peptide motifs.

AB - We report on the self-assembly mechanism and dynamics in a series of poly(γ-benzyl-L-glutamate)-b-poly(glycine) (PBLG-b-PGly) diblock copolymers within the composition range 0.67 ≤ fPBLG ≤ 0.97 and the temperature (T) range 303 < T < 433 K. Small- and wide-angle X-ray scattering, 13C NMR, and differential scanning calorimetry are used for the structure investigation coupled with dielectric spectroscopy for both the peptide secondary structure and the associated dynamics. These techniques provide not only the nanophase morphology but also the type and persistence of peptide secondary structures. The thermodynamic confinement of the blocks within the nanodomains and the disparity in their packing efficiency results in multiple chain folding of the PGly secondary structure that effectively stabilize a lamellar morphology for high fPBLG. Nanoscale confinement proves to be important in controlling the persistence length of secondary peptide motifs.

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JF - Biomacromolecules

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Nanodomain-induced chain folding in poly(γ-benzyl-L-glutamate)-b-polyglycine diblock copolymers

Abstract

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