PubMed · 2512849
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M A Abdallah, M Pfestorf, G Döring. 1989. Pseudomonas aeruginosa pyoverdin: structure and function.. https://doi.org/10.1159/000417597
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Four diamino acid-Nalpha-substituted oligopeptide (DNO) oligomers substituted with pyrenyl as photophysical probes were synthesized. The excimer formation and ground-state association of the pyrenyl groups were investigated by means of absorption and steady-state fluorescence spectroscopy together with time-resolved fluorescence techniques. The photophysical parameters obtained from the different derivatives reflect the secondary structural properties of the DNO backbones.
The solid-state structure of a heterochiral peptide embodying a D-aminosuccinyl peptide (D-Asu) and a D-Ala was studied in order to analyse the effects of Asu and amino acids with inverse chirality on peptide conformation. The crystal structure has been determined by X-ray diffraction techniques and refined to a final R factor of 0.043. The molecule adopts an unusual overall "S-shape' conformation due to two consecutive type II beta-turns. In this molecule it is possible to compare a type II beta-bend conformation (L-Ala1-D-Ala2) favoured by the presence of a D-residue at second corner to a type II beta-turn (D-Asu3-Gly4) favoured by the presence of a D-Asu residue at first corner. In agreement with previous studies, this structure confirms that the Asu has a high propensity to adopt a type II or II' beta-bend conformation and that it may be used as a strong determinant of these structural motifs.
Gln-Val-Val-Ala-Gly is a sequence which is common in cysteine protease inhibitors. Poly(ethylene glycol) hybrids of Gln-Val-Val-Ala-Gly analogs were prepared by the solid phase method by fluorenylmethyloxycarbonyl chemistry. The hybrid formation of Gln-Val-Val-Ala-Gly resulted in improvement of the solubility and also in enhancement of the inhibitory effect of the peptide on papain. In addition, the hybrid formation of Gln-Val-Val-Ala-Gly analogs resulted in the enhancement of the inhibitory effect of the peptide analogs.