Activation of lignin by selective oxidation: An emerging strategy for boosting lignin depolymerization to aromatics.

Lignin is the most abundant, renewable aromatic resource on earth and holds great potential for the production of value-added chemicals. The efficient valorization of lignin requires to deal with several formidable challenges, especially to prevent it from re-condensation reactions during its depolymerization. Recently, a strategy involving the activation of lignin side chains by selective oxidation of the benzylic alcohol in ß-O-4 linkages to facilitate lignin degradation to aromatic monomers has become very popular. This strategy provides great advantages for lignin selective degradation to high yields of aromatics under mild conditions, but requires an additional pre-oxidation step. The purpose of this review is to provide the latest cutting-edge innovations of this novel approach. Various catalytic systems, including those using chemo-catalytic methods, physio-chemo catalytic methods, and/or bio-catalytic methods, for the oxidative activation of lignin side chains are summarized. By analyzing the current situation of lignin depolymerization, certain promising directions are emphasized.

[Study on application of multi-wavelength LED array induced fluorescence spectrum in multicomponent analysis].

The technique of fluorescence spectrum is one of the efficient methods for monitoring and identifying dissolved organic matter, oil pollutants and biomass of phytoplankton in water. A new kind of fluorescence spectrum system with a multi-wavelength LED array as the exciting light source is introduced. The principle of the system and the method for multi-component analysis are discussed. The excitation-emission matrix (EEM) fluorescence spectra of samples mixed with different concentration fluorescent dyes were measured with this system in the authors' laboratory, which were analyzed using parallel factor (PARAFAC) algorithm. The results indicate that the correlation coefficient of the resolved concentration and actual ones is up to 98%, which shows the potential application of the fluorescence spectrum system in multi-component analysis.

Characterization of a single-chain variable fragment (scFv) antibody directed against the human asialoglycoprotein receptor.

To obtain scFv (single-chain variable fragment) against human ASGPR (asialoglycoprotein receptor), a human non-immune phage antibody library was screened with the recombinant CRD (carbohydrate recognition domain) of rCRDH1 (the H1 subunit of human ASGPR). Anti-rCRDH1 phage clones were obtained after four rounds of screening with rCRDH1-coated immunotubes and single positive colonies were further selected with the expressed thioredoxin-His-S tag of the wild-type pET32c. Two specific anti-rCRDH1 phage clones (named C1 and C2) were transfected into Escherichia coli HB2151 and induced for secreted expression of scFv antibody. The purified anti-rCRDH1 C1 and C2 single-chain antibodies were characterized by immunoblotting and immunohistochemistry. Both antibodies were found to specifically recognize denatured and native forms of the ASGPR and thus could potentially be used as targeting molecules for gene therapy of hepatocellular carcinoma or other liver diseases.

The C-terminal tail of presenilin regulates Omi/HtrA2 protease activity.

Presenilin mutations are responsible for most cases of autosomal dominant inherited forms of early onset Alzheimer disease. Presenilins play an important role in amyloid beta-precursor processing, NOTCH receptor signaling, and apoptosis. However, the molecular mechanisms by which presenilins regulate apoptosis are not fully understood. Here, we report that presenilin-1 (PS1) regulates the proteolytic activity of the serine protease Omi/HtrA2 through direct interaction with its regulatory PDZ domain. We show that a peptide corresponding to the cytoplasmic C-terminal tail of PS1 dramatically increases the proteolytic activity of Omi/HtrA2 toward the inhibitor of apoptosis proteins and beta-casein and induces cell death in an Omi/HtrA2-dependent manner. Consistent with these results, ectopic expression of full-length PS1, but not PS1 lacking the C-terminal PDZ binding motif, potentiated Omi/HtrA2-induced cell death. Our results suggest that the C terminus of PS1 is an activation peptide ligand for the PDZ domain of Omi/HtrA2 and may regulate the protease activity of Omi/HtrA2 after its release from the mitochondria during apoptosis. This mechanism of Omi/HtrA2 activation is similar to the mechanism of activation of the related bacterial DegS protease by the outer-membrane porins.

Structural and functional study of the apelin-13 peptide, an endogenous ligand of the HIV-1 coreceptor, APJ.

The APJ receptor is widely expressed in the human central nervous system (CNS). Apelin was recently identified as the endogenous peptidic ligand for human APJ. Studies with animal models suggested that APJ and apelin play an important role in the hypothalamic regulation of water intake and the endocrine axis, in the regulation of blood pressure, and in cardiac contractility. Apelin has been found to block the activity of APJ as a human immunodeficiency virus type I (HIV-1) coreceptor. In this study, we combined chemical synthetic approaches with alanine substitution to evaluate the structural requirements for interactions with the APJ receptor. We demonstrated that apelin peptides in aqueous solution adopt a random conformation, and the positive charge and hydrophobic residues of apelin-13 play important roles in interactions with the APJ receptor. We have observed an important correlation between receptor binding affinity and cell-cell fusion inhibitory activity. The elucidation of structural requirements of apelin-13 in its interaction with the APJ receptor is critical for further investigation of apelin-APJ functions in vivo and in the design of small molecular inhibitors for potential treatment of HIV-1 infection in the CNS.

Potent suppression of viral infectivity by the peptides that inhibit multimerization of human immunodeficiency virus type 1 (HIV-1) Vif proteins.

Virion infectivity factor (Vif) is essential for the replication of human immunodeficiency virus type 1 (HIV-1) in vivo, but its function remains uncertain. Recently, we have shown that Vif proteins are able to form multimers, including dimers, trimers, or tetramers. Because the multimerization of Vif proteins is required for Vif function in the viral life cycle, we propose that it could be a novel target for anti-HIV-1 therapeutics. Through a phage peptide display method, we have identified a set of 12-mer peptides containing a PXP motif that binds to HIV-1 Vif protein. These proline-enriched peptides potently inhibited the Vif-Vif interaction in vitro. We have also screened a set of synthesized Vif peptides (15-mer), which covers all the amino acids of the HIV-1 Vif protein sequence, for their ability to inhibit the Vif-Vif interaction in vitro. We demonstrated that Vif-derived proline-enriched peptides that contain the (161)PPLP(164) domain are able to inhibit the Vif-Vif interaction. Conversely, the deletion of the (161)PPLP(164) domain of Vif protein will significantly impair the capability of Vif proteins to interact with each other, indicating that the (161)PPLP(164) domain plays a key role in Vif multimerization. All these results demonstrate that the proline-enriched peptides block the multimerization of Vif through interfering with the polyproline interfaces of Vif formed by (161)PPLP(164) domain. Moreover, these peptides which inhibit the Vif-Vif interaction in vitro potently inhibit HIV-1 replication in the "nonpermissive" T-cells. We propose that this study starts a novel strategy to develop structural diverse inhibitors of Vif such as peptidomimetics or small organic molecules.