Screw‐sense inversion characteristic of α‐helical poly(β‐<i>p</i>‐chlorobenzyl <scp>L</scp>‐aspartate) and comparison with other related polyaspartates

Abe, Akihiro; Hiraga, Keijiro; Imada, Yousuke; Hiejima, Toshihiro; Furuya, Hidemine

doi:10.1002/bip.20207

Cited by 22 publications

(20 citation statements)

References 38 publications

(49 reference statements)

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“…In this connection, a few publications have recently reported very stimulating results on the preferred helical handedness of homo‐oligopeptides based on C α ‐ tetra substituted α‐amino acids with only side‐chain chirality 63–66. As far as the large field of helical oligo‐ and polypeptides formed by C α ‐ tri substituted α‐amino acids is concerned, only a limited number of scattered data is available,3–5, 7–10, 67–78 which does not allow one to extract a general picture of this important 3D‐structural issue.…”

Section: Resultsmentioning

confidence: 99%

Handedness control of peptide helices by amino acid side‐chain chirality: Ile/aIle peptides

et al. 2006

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A set of four hexapeptide sequences, each characterized by four strongly helicogenic Aib residues and all combinations of two isomeric Ile/aIle residues at positions 2 and 5, was synthesized by solution methods and fully characterized. A detailed solution (by FT-IR absorption, NMR, and CD techniques) and solid/crystalline state (by X-ray diffraction) conformational investigation allowed us to validate our assumption that all four peptides are folded in well-developed 3(10)-helical structures. However, the most relevant conformational conclusion extracted from the present 3D-analysis is that the handedness of the 3(10)-helical structures formed does not seem to be sensitive to the configurational change at the beta-carbon atom of the constituent Ile versus the diastereomeric aIle residues (in other words, the dominant control on this important structural parameter appears to be exerted by the chirality of the amino acid alpha-carbon atom). These results complement published findings on the diverging relative stabilities of the intermolecularly H-bonded beta-sheet structures generated by Ile versus aIle homo-oligopeptides.

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Section: Resultsmentioning

confidence: 99%

Handedness control of peptide helices by amino acid side‐chain chirality: Ile/aIle peptides

et al. 2006

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“…We should mention here that the majority of a-helices in polypeptides is right-handed although there are some examples of left-handed polypeptides. In the case of polyaspartates [60] the energy difference between right-and left-handed helices is small enough to allow a transformation between the two forms at ordinary temperatures. It is thought that this transformation mechanism involves unwinding and rewinding without an intermediate random coil.…”

Section: Persistence Length Of A-helicesmentioning

confidence: 98%

Self‐Assembly and Dynamics of Polypeptides

Floudas¹,

Spiess²

2009

Macromol. Rapid Commun.

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This work highlights the results of recent efforts to understand the hierarchical self-assembly and dynamics of polypeptides with the aid of different NMR techniques, X-ray scattering, and dielectric spectroscopy. The concerted application of these techniques sheds light on the origin of the glass transition, the persistence of the α-helical peptide secondary motif, and the effects of topology and packing on the type and persistence of secondary structures. With respect to the freezing of the dynamics at the liquid-to-glass temperature it was found that the origin of this effect is a network of defected hydrogen bonds. The presence of defected hydrogen-bonded regions reduces the persistence length of α-helices. Block copolypeptides provide means to manipulate both the type and persistence of peptide secondary structures.

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“…Poly‐ l ‐aspartic acid esters are known to be versatile and therefore being able to form either a right‐ or left‐handed α‐helix depending on the ester group . Poly‐β‐phenethyl‐ l ‐aspartate (PPLA) is known to form right‐handed helices, whereas poly‐β‐benzyl‐ l ‐aspartate (PBLA) preferably forms left‐handed helices . By incorporation of BLA residues in PPLA, copolymers of PPLA and PBLA are obtained, which show a much lower helix reversal temperature than mere PPLA.…”

Section: Figurementioning

confidence: 99%

Thermoresponsive Alignment Media in NMR Spectroscopy: Helix Reversal of a Copolyaspartate at Ambient Temperatures

Schwab

Schmidts

Thiele

2018

Chemistry A European J

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Poly(aspartic acid esters) are known to form either right-or left-handed α-helices depending on the ester group in the side chain, on solvent and/or on temperature. Polyphenethyl-l-aspartates (PPLA) exhibit a helix reversal from the right- to the left-handed form with increasing temperature. We have recently reported the application of polyphenethylaspartates as helically chiral alignment media. The thermoresponsivity observed for these polymers offers the possibility to measure different orientations of analytes before and after helix reversal of the alignment medium at 373 K. Herein we present a synthesized copolymer of phenethyl- and benzylaspartate as a new alignment medium undergoing this helix reversal at 303-313 K. Thus, the measurement of residual dipolar couplings (RDC) before and after the helix reversal is allowed for at ambient temperatures. A complete sign change of all H- C RDCs was observed, which is close to the highest possible difference in NMR spectra.

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Screw‐sense inversion characteristic of α‐helical poly(β‐p‐chlorobenzyl L‐aspartate) and comparison with other related polyaspartates

Abstract: This is one of a series of studies on the reversal of the helix sense of polyaspartates originated from the pioneering work of Goodman and his associates in 1960s. Poly(␤-p-chlorobenzyl L-aspartate) (PClBLA)

Cited by 22 publications

References 38 publications

Handedness control of peptide helices by amino acid side‐chain chirality: Ile/aIle peptides

Handedness control of peptide helices by amino acid side‐chain chirality: Ile/aIle peptides

Self‐Assembly and Dynamics of Polypeptides

Thermoresponsive Alignment Media in NMR Spectroscopy: Helix Reversal of a Copolyaspartate at Ambient Temperatures

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