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Vibrational spectroscopic analysis of LD ‐sequential, bacterial cell wall peptides: An IR and raman study
Author(s) -
Naumann Dieter,
Labischinski Harald,
Rönspeck Wolfgang,
Barnickel Gerhard,
Bradaczek Hans
Publication year - 1987
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.360260603
Subject(s) - chemistry , raman spectroscopy , amide , dipeptide , pentapeptide repeat , crystallography , hydrogen bond , aqueous solution , stereochemistry , infrared spectroscopy , peptide , molecule , organic chemistry , biochemistry , physics , optics
The synthetic, zwitterionic bacterial cell wall peptides— D ‐Glu γ ‐L‐Lys, D ‐Glu γ ‐L‐Lys‐ D ‐Ala, D ‐Glu γ ‐L‐Lys‐ D ‐Ala‐ D ‐Ala, and L‐Ala‐ D ‐Glu γ ‐L‐Lys‐ D ‐Ala‐ D ‐Ala—have been investigated in the crystalline and aqueous solution state applying ir and Raman spectroscopy. Additionally, aqueous solutions of the tetra‐ and pentapeptide have been investigated by CD spectroscopic techniques. Apart from the dipeptide, whose spectral features were dominated by end‐group vibrations, the corresponding ir and Raman active bands of the crystalline peptides in the amide and skeletal regions were found at similar wave numbers, thus suggesting an analogous three‐dimensional structure of these compounds. Dominant amide A, I, II, and III bands near 3275, 1630, 1540, and 1220–1250 cm −1 , respectively, in the ir are interpreted in favor of an intermolecularly hydrogen‐bonded, β‐like structure. The absence of any amide components near 1680–1690 cm −1 , together with the presence of strong amide bands near 1630 cm −1 , and weak bands near 1660 cm −1 in the ir, which, conversely, were found in the Raman spectra as weak and strong bands, but at corresponding wave numbers, is taken as strong evidence for the presence of the unusual, parallel‐arranged β‐structure. On the basis of comparative theoretical considerations, a parallel‐arranged, “β‐type ring” conformation [P. De Santis, S. Morosetti, and R. Rizzo (1974) Macromolecules 7 , 52–58] is hypothesized. The solubilized peptides exhibited distinct similarities with their crystalline counterparts in respect to frequency values and relative intensities of the corresponding ir and Raman‐active amide I/I′ components, and of some Raman bands in the skeletal region. This is interpreted in terms of residual short‐range order, persisting even in aqueous solution. We concluded that the peptides show a strong propensity to form hydrated, strongly associated aggregates in water. On the basis of amide I/I′ band positions, stable, intramolecular interactions via the amide groups are discarded for the solubilized peptides. Complementarily, the CD data obtained suggest the presence of weakly bent, “open‐turn”‐like structures for the tetra‐ and pentapeptide in aqueous solution.