New structures of <scp>LD</scp>‐alternating polypeptides in solution and in the solid state

Ascoli, Franca; Angelis, G. de; Bianco, Federica; Santis, P. De

doi:10.1002/bip.1975.360140518

Cited by 15 publications

(11 citation statements)

References 7 publications

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“…[21] Early studies of synthetic b-helices focused on syndiotactic homopolydipeptides. [38,39] In particular, X-ray and electron fiber diffraction studies of poly-g-benzyl-d,l-glutamate demonstrated that the polymer can exist in not only single-but also double-stranded b-helical conformations. [40,41] While double-or higher stranded helical structures had long been known for polynucleotides and certain polysaccharides, these were the first such structures documented for polypeptides.…”

Section: Linear Dl-peptides Form Cylindrical B-or P DL -Helicesmentioning

confidence: 99%

“…[41] In 1975 DeSantis and co-workers reported the first attempts at preparing b-helix-forming oligopeptides of discrete length. [39] In the solid state, peptides of general sequence X(l-Ala-d-Val) m Y displayed X-ray powder diffraction patterns consistent with a-pleated structures [28,29,42] while circular dichroism (CD) spectra of the polymer in trifluoroethanol (TFE) suggested a b-helical conformation. In addition, 1 H NMR spectra ([D 6 ]DMSO) of hexa-and octapeptides (X benzyloxycarbonyl (Cbz), Y OMe) were well dispersed and showed 3 J NH,aH values of nearly 8.5 Hz, which strongly evince b-type f torsion angles.…”

Section: Linear Dl-peptides Form Cylindrical B-or P DL -Helicesmentioning

confidence: 99%

See 1 more Smart Citation

Self-Assembling Organic Nanotubes

Bong

Clark

Granja

et al. 2001

Angew. Chem. Int. Ed.

1,079

130

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Section: Linear Dl-peptides Form Cylindrical B-or P DL -Helicesmentioning

confidence: 99%

Section: Linear Dl-peptides Form Cylindrical B-or P DL -Helicesmentioning

confidence: 99%

Self-Assembling Organic Nanotubes

Bong

Clark

Granja

et al. 2001

Angew. Chem. Int. Ed.

1,079

130

View full text Add to dashboard Cite

“…The roles that various structural factors can have in the conformations of l , d ‐peptides, such as the length of the chain, the nature of the side chains, and the specific configuration motif ( dld or ldl ), were investigated. To this end, l , d ‐α‐peptides with different sequences and lengths were synthesized and their conformational properties were investigated …”

Section: Synthetic Ld‐peptides As Models Of Ion Channels and Carriersmentioning

confidence: 99%

“…The linear l , d ‐octapeptide Cbz‐( l ‐Ala‐ d ‐Val) 4 ‐OCH 3 was proposed as an ion channel model under the hypothesis that the expansion of the pattern l ‐Ala‐ d ‐Val could reproduce the main features of gramicidin A . Experimental findings demonstrated that Cbz‐( l ‐Ala‐ d ‐Val) 4 ‐OCH 3 adopts single‐strand β‐like conformations.…”

Section: Synthetic Ld‐peptides As Models Of Ion Channels and Carriersmentioning

confidence: 99%

Peptides with regularly alternating enantiomeric sequence: From ion channel models to bioinspired nanotechnological applications

et al. 2018

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Peptides are versatile building blocks that have been extensively used as peptide‐based organizers to generate bioinspired hybrid materials. Among them, those peptides characterized by regularly alternating enantiomeric sequences (l,d‐peptides) have attracted much interest. Their structures, which are not accessible to the corresponding homochiral peptides, have been exploited to achieve hybrid conjugates, the chemical and structural properties of which can be predetermined by correct design. Molecules that self‐assemble into hollow tubular architectures with side chains on the outer surface can form, allowing the introduction of new functionalities on amino acid residues containing reactive side chains. This provides an effective strategy to develop engineered nanotubes with the surface suitably tuned for applications in different fields, spanning from electronics to medicine.

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“…(2::;:; n::;:; 8), (Ala-Alao-Ala-o-Ala). (2::;:; n::;:; 6) and (Ala-Ala-Ala-o-Ala). (2 ;2; n::;:; 7) give broad infrared bands at about 650 em_, (Figures 3(B), (C) and (D), 4(B), (C), and (D)', and 5(B), (C) and (D)), which can be assigned to the amide V mode of the· random-coil structure.…”

Section: Raman Spectramentioning

confidence: 99%

Conformational Study of Sequential Polypeptides of L-Alanine and D-Alanine

Ozaki

Oya

Itoh

1981

Polym J

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Infrared spectra in the 700-200 em -J and in the amide I and II regions were measured for poly(L-Ala-L-Ala-n-Ala), poly(L-Ala-L-Ala-n-Ala-n-Ala), poly(L-Ala-L-Ala-L-Ala-D-Ala), and poly(L-Ala-n-Ala-L-Ala-n-Ala) with different degrees of polymerization. The spectra showed that the films cast from aqueous solutions ofpoly(L-Ala-L-Aia-n-Aia), poly(L-Aia-L-Ala-D-Ala-n-Ala), and poly(L-Aia-L-Ala-L-Aia-n-Aia) take disordered conformations containing appreciable amounts ofL-alanine residues with local right-handed a-helix-like structures and then-alanine residues with local left-handed a-helix-like structures. The disordered conformations were converted to the extended {J-form when treated with ethanol. The latter conformation is also found in waterinsoluble portions of poly(L-Ala-L-Aia-n-Ala-n-Aia) and poly(L-Ala-L-Ala-L-Aia-n-Ala). On the other hand, poly(L-Ala-n-Ala-L-Aia-n-Aia) has a conformation different from those taken on other sequential polypeptides studied in this paper. The above findings were confirmed also by the measurement of the Raman spectra of poly(L-Ala-L-Ala-n-Aia) and poly(L-Ala-n-Ala-L-Aia-D-Ala).

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New structures of LD‐alternating polypeptides in solution and in the solid state

Cited by 15 publications

References 7 publications

Self-Assembling Organic Nanotubes

Self-Assembling Organic Nanotubes

Peptides with regularly alternating enantiomeric sequence: From ion channel models to bioinspired nanotechnological applications

Conformational Study of Sequential Polypeptides of L-Alanine and D-Alanine

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