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The α-helical conformation of the undecapeptide boc-l-Ala-[Aib-Ala]2-Glu(OBzl)-Ala-[Aib-Ala]2-OMe: Synthesis, X-Ray crystal structure, and conformation in solution

✍ Scribed by Schmitt, Heribert ;Winter, Werner ;Bosch, Roland ;Jung, Günther

Publisher
John Wiley and Sons
Year
1982
Tongue
English
Weight
934 KB
Volume
1982
Category
Article
ISSN
0947-3440

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✦ Synopsis

As models of the helical N-terminal part of alamethicin the undecapeptides Boc-L-Ala-[Aib-Ala]2-Glu(0Bzl)-Ala-[Aib-Ala],-OMe (1) and Boc-~-Ala-[Aib-Ala]~-Gly-Ala-[Aib-Ala]~-OMe (2) were synthesized. 1 was examined by X-ray crystallography using direct methods for solution of the phase problem. The unit cell (P2,) contains two antiparallel a-helices with nine residues being part of the helix. Continuing chains of head-to-tail linked a-helices are arranged in the crystal lattice. C D and I3C NMR spectra revealed a pronounced stabilizing effect of the cc-aminoisobutyric acid residues for the a-helical conformation in solution.

📜 SIMILAR VOLUMES

Crystal structure of the α-helical undec
Crystal structure of the α-helical undecapeptide Boc-L-Ala-Aib-Ala-Aib-Ala-Glu(OBzl)-Ala-Aib-Ala-Aib-Ala-OMe
✍ R. Bosch; G. Jung; H. Schmitt; W. Winter 📂 Article 📅 1985 🏛 Wiley (John Wiley & Sons) 🌐 English ⚖ 783 KB

## Abstract The x‐ray structure of Boc‐L‐Ala‐Aib‐Ala‐Aib‐Ala‐Glu(OBzl)‐Ala‐Aib‐Ala‐Aib‐Ala‐OMe(I) represents the first α‐helix determined by direct methods. This undecapeptide is a model of the N‐terminus of alamethicin, and it exhibits voltage‐dependent pores in bilayer membranes at a higher volta

Conformation of Boc-L-Ala-Aib-L-Ala-OMe
Conformation of Boc-L-Ala-Aib-L-Ala-OMe in the Crystal and in Solution
✍ Bosch, Roland ;Jung, Günther ;Voges, Klaus-Peter ;Winter, Werner 📂 Article 📅 1984 🏛 John Wiley and Sons 🌐 English ⚖ 560 KB

## Abstract Boc‐L‐Ala‐Aib‐L‐OMe (**1**) crystallizes in the space group __P__2~1~ with __a__ = 11.732(1), __b__ = 6.013(1), __c__ = 14.195(2) Å, β = 91.76(1)→, and Z = 2(__R__ value for 3089 reflexions: 0.047). The peptide adopts a new type of β‐turn with a very wide 4→1 hydrogen bond distance of 3

Circular dichroism and conformational an
Circular dichroism and conformational analysis of the membrane-modifying peptide -N-t-Boc-(Aib-L-Ala)5-Gly-Ala-Aib-Pro-Ala-Aib-Aib-Glu-(OBzl)-Gln-OMe with respect to alamethicin
✍ R. Oekonomopulos; G. Jung 📂 Article 📅 1980 🏛 Wiley (John Wiley & Sons) 🌐 English ⚖ 665 KB

## Abstract The conformational analysis of the CD spectrum is reported for the synthetic and membrane‐modifying nonadecapeptide analog of alamethicin __N__‐__t__‐Boc‐(Aib‐L‐Ala)~5~‐Gly‐Ala‐Aib‐Pro‐Ala‐Aib‐Aib‐Glu(OBzl)‐ Gln‐OMe. The CD data are evaluated according to three different methods and are

Conformation of peptides containing α-Am
Conformation of peptides containing α-Aminoisobutyric acid the crystal structure of Boc-Gly-l-Ala-Aib-OMe
✍ Bosch, Roland ;Jung, Günther ;Winter, Werner 📂 Article 📅 1982 🏛 John Wiley and Sons 🌐 English ⚖ 396 KB

## Abstract Boc‐Gly‐L‐Ala‐Aib‐OMe (**1**) crystallizes in the space group __P__2~1~2~1~2~1~ with __a__ = 10.043(3), __b__ = 11.590(5), __c__ = 16.779(1) Å, and __Z__ = 4 (__R__ value for 1859 symmetry independent reflexions: 0.043). On the basis of a 4 → 1 intramolecular hydrogen bond, the tripepti