481 research outputs found

    Lectins as Plant Defense Proteins

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    Developmental Regulation of Lectin and Alliinase Synthesis in Garlic Bulbs and Leaves

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    Brassica juncea chitinase BjCHI1 inhibits growth of fungal phytopathogens and agglutinates Gram-negative bacteria

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    Brassica juncea BjCHI1 is a plant chitinase with two chitin-binding domains. Its expression, induced in response to wounding, methyl jasmonate treatment, Aspergillus niger infection, and caterpillar Pieris rapae feeding, suggests that it plays a role in defence. In this study, to investigate the potential of using BjCHI1 in agriculture, Pichia-expressed BjCHI1 and its deletion derivatives that lack one or both chitin-binding domains were tested against phytopathogenic fungi and bacteria. Transplastomic tobacco expressing BjCHI1 was also generated and its extracts assessed. In radial growth-inhibition assays, BjCHI1 and its derivative with one chitin-binding domain showed anti-fungal activities against phytopathogens, Colletotrichum truncatum, C. acutatum, Botrytis cinerea, and Ascochyta rabiei. BjCHI1 also inhibited spore germination of C. truncatum. Furthermore, BjCHI1, but not its derivatives lacking one or both domains, inhibited the growth of Gram-negative bacteria (Escherichia coli, Ralstonia solanacearum, Pseudomonas aeruginosa) more effectively than Gram-positive bacteria (Micrococcus luteus and Bacillus megaterium), indicating that the duplicated chitin-binding domain, uncommon in chitinases, is essential for bacterial agglutination. Galactose, glucose, and lactose relieved agglutination, suggesting that BjCHI1 interacts with the carbohydrate components of the Gram-negative bacterial cell wall. Retention of chitinase and bacterial agglutination activities in transplastomic tobacco extracts implicates that BjCHI1 is potentially useful against both fungal and bacterial phytopathogens in agriculture

    Exciton bimolecular annihilation dynamics in supramolecular nanostructures of conjugated oligomers

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    We present femtosecond transient absorption measurements on π\pi-conjugated supramolecular assemblies in a high pump fluence regime. Oligo(\emph{p}-phenylenevinylene) monofunctionalized with ureido-\emph{s}-triazine (MOPV) self-assembles into chiral stacks in dodecane solution below 75∘^{\circ}C at a concentration of 4×10−44\times 10^{-4} M. We observe exciton bimolecular annihilation in MOPV stacks at high excitation fluence, indicated by the fluence-dependent decay of 111^1Bu_{u}-exciton spectral signatures, and by the sub-linear fluence dependence of time- and wavelength-integrated photoluminescence (PL) intensity. These two characteristics are much less pronounced in MOPV solution where the phase equilibrium is shifted significantly away from supramolecular assembly, slightly below the transition temperature. A mesoscopic rate-equation model is applied to extract the bimolecular annihilation rate constant from the excitation fluence dependence of transient absorption and PL signals. The results demonstrate that the bimolecular annihilation rate is very high with a square-root dependence in time. The exciton annihilation results from a combination of fast exciton diffusion and resonance energy transfer. The supramolecular nanostructures studied here have electronic properties that are intermediate between molecular aggregates and polymeric semiconductors

    Exciton/Charge-transfer Electronic Couplings in Organic Semiconductors

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    Charge transfer (CT) states and excitons are important in energy conversion processes that occur in organic light emitting devices (OLEDS) and organic solar cells. An ab initio density functional theory (DFT) method for obtaining CT−exciton electronic couplings between CT states and excitons is presented. This method is applied to two organic heterodimers to obtain their CT−exciton coupling and adiabatic energy surfaces near their CT−exciton diabatic surface crossings. The results show that the new method provides a new window into the role of CT states in exciton−exciton transitions within organic semiconductors.United States. Dept. of Energy (DEFG02- 07ER46474)David & Lucile Packard Foundation (Fellowship
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