Critical chain length for the formation of α- and β-polypeptide conformations in the solid state. Syntheses and conformations of oligopeptides with alternateL-alanyl andL-leucyl residues

Author(s):  
Ryoichi Katakai
1987 ◽  
Vol 52 (5) ◽  
pp. 1356-1361
Author(s):  
S. Abdel Rahman ◽  
M. Elsafty ◽  
A. Hattaba

The conformation of elastin-like peptides Boc-Ala-Pro-Gly-Val-APEGM, Boc-Ala-Pro-Gly-Val-Gly-Val-APEGM, Boc-Ala-Pro-Gly-Val-Ala-Pro-Gly-Val-Gly-Val-APEGM, Boc-Ala-Pro-Gly-Val-Gly-Val-Ala-Pro-Gly-Val-Gly-Val-APEGM were examined in solution using circular dichroism at 30 °C, 50 °C, and 70 °C and in solid state by IR at room temperature. The studies show that the β-turn is a significant conformational feature for peptides under investigation in solution at 30 °C and 50 °C, but at 70 °C the tetra, hexa, and decapeptides show the CD feature characteristic of the β-structure while the dodecapeptide spectra show the presence of β-turn which indicates the stability of the β-turn at this chain length. The IR spectra show that in the solid state at room temperature all investigated peptides assume essentially a β-turn except the tetrapeptide which present evidence of antiparallel β-structure. The β-turn contribution in the IR spectra increases with the increase of the chain length of the peptide.


Polymer ◽  
2004 ◽  
Vol 45 (12) ◽  
pp. 4009-4015 ◽  
Author(s):  
Bin Zhang ◽  
Shanju Zhang ◽  
Lidia Okrasa ◽  
Tadeusz Pakula ◽  
Tim Stephan ◽  
...  

Nano Letters ◽  
2005 ◽  
Vol 5 (7) ◽  
pp. 1315-1320 ◽  
Author(s):  
Lukas Schmidt-Mende ◽  
Jessica E. Kroeze ◽  
James R. Durrant ◽  
Md. K. Nazeeruddin ◽  
Michael Grätzel

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