## Abstract The β‐defensins comprise a large family of small cationic antimicrobial peptides widely distributed in plants, mammals and insects. These cysteine rich peptides display multifunctional properties with implications as potential therapeutic agents. Recent research has highlighted their ro
Structure-Activity Relationships in Peptide Juvenoids
✍ Scribed by J. Hlavacek; J. Koudelka; J. Jarv
- Publisher
- Elsevier Science
- Year
- 1993
- Tongue
- English
- Weight
- 263 KB
- Volume
- 21
- Category
- Article
- ISSN
- 0045-2068
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✦ Synopsis
The structure-activity relationships for selected peptide juvenoids of the general formula (\mathrm{R}^{1}-\mathrm{CONHCH}\left(\mathrm{R}^{3}\right) \mathrm{CONH}-\mathrm{C}{6} \mathrm{H}{4}-\mathrm{R}^{2}) were analyzed by using linear free energy relationships. It was found that both the hydrophobicity and the inductive effect of the amino-terminal substituent (\mathrm{R}^{1}) of these compounds, quantified by the constants (\pi) and (\sigma^{*}), are important factors for recognition of the peptide juvenoids by their putative "target site" in the insect body and that these effects are independent of the structure of the rest of the juvenoid molecule. In contrast, the mechanism of interaction of the amino acid side chain (R^{3}) with the target site depends upon the structure of other substituents that explain the synergistic effects in juvenoid action. (e 1993 Academic Press. Inc.
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