Puroindoline B |
puromycin-insensitive leucyl-specific aminopeptidase |
IL1 receptor R2 |
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Puroindoline A and Puroindoline B are two basic and cystine-rich proteins with a unique tryptophan-rich domain, isolated from wheat endosperm (Gautier et al, 1994; Blochet et al, 1993). The proteins are lipid-binding proteins and determine grain texture.
The purified or expressed proteins also exhibit various degrees of antimicrobial activity against several Gram-positive bacteria and Gram-negative bacteria and/or fungi (Capparelli et al, 2005; Miao et al, 2012), including Staphylococcus epidermidis (Capparelli et al, 2007). Studies with transgenic plants show that they are antifungal (Krishnamurthy et al, 2001; Faize et al, 2004; Luo et al, 2008) and may play a role in vivo in seed defence (Kim et al, 2012). Synthetic peptides mimicking the tryptophan-rich
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