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• W160996461 abstract "ABSTRACT Pardaxin, the toxic compound from the secretion of the Red Sea flatfish Pardachirus marmoratus has been examined by Raman and circular dichroism techniques. Conformational information regarding the peptide backbone, disulfide bond and tyrosine chromophores was obtained. The Amide I band appeared at 1658 cm −1 as a strong, discrete band and the Amide III appeared at 1280 cm −1 . Analysis of the Raman spectra by the method of Lippert and colleagues (1976) shows that the toxin consists of 39% α-helix, 23% β-structure and 39% random coil. The Lippert equation does not include the β-turn term; therefore, the content of β-reverse turn could not be obtained. The occurrence of a band at 510-512 cm −1 indicates the conformational geometry of the disulfide C-C-S-S-C-C linkages to be gauche-gauche-gauche. The lack of -SH stretching vibration in the region of 2500 ∼ 2700 cm −1 region indicates that all half-cystines are used in disulfide linkages. The far-UV CD spectrum showed the positive 196 and negative 208 and 222 nm bands. Pardaxin possesses quite unusual helical structure which does not fit the models based on the quantitatively estimated secondary structure. The best fit secondary structure based on CD ellipticity by the method of Chen and colleagues (1972) was found to be: 23% α-helix, 21% β-structure and 56% random. At the most acidic and alkaline pH the far-UV Pardaxin spectra showed extensive loss of its helical structure, which was found to be reversible. Examination of the near-UV CD spectrum showed the existence of phenylalanine and tyrosine bands. Since Pardaxin toxicity to fish is enhanced when the toxin is applied in media containing very high NaCl concentrations, the possible influence of salt on Pardaxin's secondary structure was tested. From the examination of the far-UV CD and Raman spectra it appears that salt does not alter the structural conformation. It is believed that the enhanced toxicity to fish in high NaCl medium concentration is due to the effect on the fish transport mechanism rather than a direct effect of the salt media on Pardaxin conformation." @default.
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• W160996461 title "CONFORMATION OF PARDAXIN, THE PURIFIED POLYPEPTIDE FROM THE TOXIC SECRETION OF THE FLATFISH PARDACHIRUS MARMORATUS STUDIED BY LASER RAMAN SPECTROSCOPY AND CIRCULAR DICHROISM" @default.
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• W160996461 doi "https://doi.org/10.1016/b978-0-08-024952-0.50063-6" @default.
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