Conformational effects on peptide aggregation in organic solvents: Spectroscopic studies of two chemotactic tripeptide analogs
✍ Scribed by P. Antony Raj; P. Balaram
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 1985
- Tongue
- English
- Weight
- 728 KB
- Volume
- 24
- Category
- Article
- ISSN
- 0006-3525
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✦ Synopsis
The aggregation behavior of the chemotactic peptide analogs, Formyl-Met-Leu-Phe-OMe (1) and Formyl-Met-AibPhe-OMe (21, has been studied in chloroform and dimethylsulfoxide over the concentration range of 0.2-110 mM by 'H-nmr spectroscopy. Both peptides associate in CDC1, at concentrations 2 2 mM, while there is no evidence for aggregation in (CD&SO. Analog 1 adopts an extended conformation in both solvents favoring association to form P-sheet structures. A folded, y-turn conformation involving a 3 -1 hydrogen bond between Met CO and Phe NH is supported by 'H-, 'Gnmr, and ir studies of analog 2. The influence of backbone conformation on the ease of peptide aggregation is demonstrated by ir studies in CHCl, and CD studies in dioxane.