Control of peptide secondary structure and dynamics in poly(γ-benzyl- L-glutamate)-b-polyalanine peptides

A. Gitsas; G. Floudas; M. Mondeshki; H. W. Spiess; T. Aliferis; H. Iatrou; N. Hadjichristidis

doi:10.1021/ma801770b

Control of peptide secondary structure and dynamics in poly(γ-benzyl- L-glutamate)-b-polyalanine peptides

A. Gitsas, G. Floudas^*, M. Mondeshki, H. W. Spiess, T. Aliferis, H. Iatrou, N. Hadjichristidis

^*Corresponding author for this work

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

40 Scopus citations

Abstract

The stability, persistence and dynamics of the peptide secondary motifs are investigated in a series of poly(γ-benzyl-L-glutamate)-b-polyalanine (PBLG-b-PAla) polypeptides through a combination of structural (X-rays, NMR) and dynamic (Dielectric Spectroscopy, NMR) probes. The unfavorable enthalpic interactions between the unlike blocks give rise to nanophase separation that results in the destabilization of PAla β-sheets. Contrary to this, the overall helicity of PBLG α-helices is enhanced. The dynamics of the "defected" amorphous segments and of the more ordered segments are studied by DS and ¹³C NMR, respectively. These probes provide information on the time scale and the mechanism of molecular and supramolecular motion.

Original language	English (US)
Pages (from-to)	8072-8080
Number of pages	9
Journal	Macromolecules
Volume	41
Issue number	21
DOIs	https://doi.org/10.1021/ma801770b
State	Published - Nov 11 2008
Externally published	Yes

ASJC Scopus subject areas

Organic Chemistry
Polymers and Plastics
Inorganic Chemistry
Materials Chemistry

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title = "Control of peptide secondary structure and dynamics in poly(γ-benzyl- L-glutamate)-b-polyalanine peptides",

abstract = "The stability, persistence and dynamics of the peptide secondary motifs are investigated in a series of poly(γ-benzyl-L-glutamate)-b-polyalanine (PBLG-b-PAla) polypeptides through a combination of structural (X-rays, NMR) and dynamic (Dielectric Spectroscopy, NMR) probes. The unfavorable enthalpic interactions between the unlike blocks give rise to nanophase separation that results in the destabilization of PAla β-sheets. Contrary to this, the overall helicity of PBLG α-helices is enhanced. The dynamics of the {"}defected{"} amorphous segments and of the more ordered segments are studied by DS and 13C NMR, respectively. These probes provide information on the time scale and the mechanism of molecular and supramolecular motion.",

author = "A. Gitsas and G. Floudas and M. Mondeshki and Spiess, {H. W.} and T. Aliferis and H. Iatrou and N. Hadjichristidis",

year = "2008",

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doi = "10.1021/ma801770b",

language = "English (US)",

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pages = "8072--8080",

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TY - JOUR

T1 - Control of peptide secondary structure and dynamics in poly(γ-benzyl- L-glutamate)-b-polyalanine peptides

AU - Gitsas, A.

AU - Floudas, G.

AU - Mondeshki, M.

AU - Spiess, H. W.

AU - Aliferis, T.

AU - Iatrou, H.

AU - Hadjichristidis, N.

PY - 2008/11/11

Y1 - 2008/11/11

N2 - The stability, persistence and dynamics of the peptide secondary motifs are investigated in a series of poly(γ-benzyl-L-glutamate)-b-polyalanine (PBLG-b-PAla) polypeptides through a combination of structural (X-rays, NMR) and dynamic (Dielectric Spectroscopy, NMR) probes. The unfavorable enthalpic interactions between the unlike blocks give rise to nanophase separation that results in the destabilization of PAla β-sheets. Contrary to this, the overall helicity of PBLG α-helices is enhanced. The dynamics of the "defected" amorphous segments and of the more ordered segments are studied by DS and 13C NMR, respectively. These probes provide information on the time scale and the mechanism of molecular and supramolecular motion.

AB - The stability, persistence and dynamics of the peptide secondary motifs are investigated in a series of poly(γ-benzyl-L-glutamate)-b-polyalanine (PBLG-b-PAla) polypeptides through a combination of structural (X-rays, NMR) and dynamic (Dielectric Spectroscopy, NMR) probes. The unfavorable enthalpic interactions between the unlike blocks give rise to nanophase separation that results in the destabilization of PAla β-sheets. Contrary to this, the overall helicity of PBLG α-helices is enhanced. The dynamics of the "defected" amorphous segments and of the more ordered segments are studied by DS and 13C NMR, respectively. These probes provide information on the time scale and the mechanism of molecular and supramolecular motion.

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U2 - 10.1021/ma801770b

DO - 10.1021/ma801770b

M3 - Article

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SN - 0024-9297

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JO - Macromolecules

JF - Macromolecules

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ER -

Control of peptide secondary structure and dynamics in poly(γ-benzyl- L-glutamate)-b-polyalanine peptides

Abstract

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