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Konformationsuntersuchungen an oligoalanin, substanz P und der myoglobinsequenz (66–73) der zirkulardichroismus von polyäthylenglykolgebundenen peptiden by M. Mutter; H. Mutter; R. Uhmann; E. Bayer is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

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## Abstract The conformation of polyethylene glycol‐bound peptides, synthesized by the liquid‐phase method, was investigated. This marcromolecular C‐terminal protecting group is transparent in the visible and the ultraviolet range to 190 nm and solubilizes peptides in many different solvents. The CD spectra of the polymer‐bound myoglobin sequence 66–73 and of the biologically active undecapeptide “substance __P__” were measured in each step of the synthesis. In both examples the formation of a secondary structure during the growth of the peptide chain was found. In the hydrophobic octapeptide containing the myoglobin sequence 66–73, the influence of either the blocked or the free N‐terminal amino group on the conformation was observed. The blocked octapeptide in trifluoroethanol showed a higher degree of α‐helix contribution than in its free state. The conformation of the polyethylene glycol‐bound nona‐ and decaalanine in trifluoroethanol and water was determined. The peptide with a free amino end group has β‐conformation in trifluoroethanol as well as in water. The corresponding N‐Boc‐protected derivatives show helical structure. The amino end group has a decisive influence on the

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Author

M. Mutter; H. Mutter; R. Uhmann; E. Bayer

Publisher

Wiley (John Wiley & Sons); John Wiley & Sons Inc.; Wiley (ISSN 0006-3525)

Published

1976

Language

DE

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)