A novel class of antimicrobial cationic polycarbonate/PEG hydrogels are designed and synthesized by Michael addition chemistry. These hydrogels demonstrate strong broad-spectrum antimicrobial activities against various clinically isolated multidrug-resistant microbes. Moreover, they exhibit nonfouling properties and prevent the substrate from microbial adhesion. These antimicrobial and antifouling gels are promising materials as catheter coatings and wound dressings to prevent infections.

Polymeric materials solely composed of certain alkylated kraft lignin preparations can be quite similar to polystyrene in tensile behavior. They may be plasticized in forming miscible blends with aliphatic polyesters possessing methylene/carboxylate group ratios (CH2/COO) of 2.0−4.0. The alkylated kraft lignin species in such materials range from individual molecular components to huge supramacromolecular associated complexes. The interactions between the alkylated kraft lignin components and polyester chains are most favorable when CH2/COO falls between 2.5 and 3.0. Under these circumstances a much smaller proportion of alkylated kraft lignin in the blend is required to disrupt the crystalline domains of the polyester than if CH2/COO were 4.0. Despite this, appreciably more aliphatic polyester is needed to plasticize the alkylated kraft lignin when CH2/COO lies between 2.5 and 3.0:  the supramacromolecular complexes tend to be dismantled to a greater extent when the plasticizer interacts more favorably with the individual kraft lignin components of which they are composed.

Poly(ethylene glycol)-block-poly(acrylic acid-co-acrylamidophenylboronic acid) [PEG(114)-b-(PAA(63)-co-PAAPBA(107))] was synthesized by the modification of poly(ethylene glycol)-block-poly(acrylic acid) (PEG(114)-b-PAA(170)) with 3-aminophenylboronic acid (APBA). Glucose-responsive PEG(114)-b-(PAA(63)-co-PAAPBA(107)) self-assembled into core-shell micelles with the hydrophobic core composed of PAAPBA and hydrophilic shell composed of PEG in aqueous solution. The swelling and disaggregating behaviors of micelles responding to glucose were investigated by using light scattering in aqueous solution at pH 7.4. Characterization of insulin-loaded micelles and their drug release in solutions with various glucose concentrations were further studied. The results demonstrated that the drug release rate can be controlled by variation of glucose concentration.

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The carbon storage regulator A (CsrA) is a protein responsible for the repression of a variety of stationaryphase genes in bacteria. In this work, we describe the nuclear magnetic resonance (NMR)-based structure of the CsrA dimer and its RNA-binding properties. CsrA is a dimer of two identical subunits, each composed of five strands, a small ␣-helix and a flexible C terminus. NMR titration experiments suggest that the ␤1-␤2 and ␤3-␤4 loops and the C-terminal helix are important elements in RNA binding. Even though the ␤3-␤4 loop contains a highly conserved RNA-binding motif, GxxG, typical of KH domains, our structure excludes CsrA from being a member of this protein family, as previously suggested. A mechanism for the recognition of mRNAs downregulated by CsrA is proposed.

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Secretory proteins and most membrane proteins are synthesized with a signal sequence that is usually cleaved from the nascent polypeptide chain, during its transport, into the lumen of the endoplasmic reticulum (ER). We have analyzed the kinetics of the cleavage of the HIV-1 Env protein signal sequence from gp160 and gp120 in HeLa, BHK, and Jurkat cells. Furthermore, we have determined the effects of this cleavage on the association of the gp160 and gp120 glycoproteins with the ER protein calnexin and the effects of the signal sequence cleavage on protein folding. The cleavage of the HIV-1 Env protein signal sequence on both gp160 and gp120 occurred very slowly in all three cell lines with a t(1/2) of 45-60 min. The core glycosylated and signal-sequence-retained forms of gp160 and gp120 associated with calnexin while the signal-sequence-cleaved forms of gp160 and gp120 had disassociated from calnexin and correctly folded as determined by their ability to associate with the CD4 cellular receptor. Further analysis of the folding state of gp160 and gp120 in nonreducing SDS-PAGE revealed that the signal-sequence-retained and calnexin-associated forms of gp160 and gp120 migrated as broad, diffuse bands, whereas the signal-sequence-cleaved or CD4-associated forms of gp160 and gp120 migrated as single sharper bands. The cause of this retardation in the rate of folding and intracellular transport of HIV-1 glycoproteins was localized to their signal sequences by fusing the vesicular stomatitis virus G protein with the HIV-1 Env protein signal sequence and expressing this chimeric protein in mammalian cells. The HIV-1 Env protein signal sequence on the VSV-G protein also confers a reduced rate of cleavage and slow intracellular transport and folding of the chimeric G protein. These results provide direct evidence that in vivo the HIV-1 glycoprotein signal sequence inhibits the folding of HIV-1 Env protein. Our data also suggest a direct correlation between the rate of the signal sequence cleavage and protein folding.

A protein-resistant surface has been constructed on the poly(methyl methacrylate) (PMMA) microfluidic chips based on a one-step modification. The copolymer of butyl methacrylate (BMA) and poly(ethylene glycol) methyl ether methacrylate (PEGMA) is synthesized to introduce a dense PEG molecular brush-like coating on the PMMA microchannel surfaces via the anchoring effect of the hydrophobic BMA units. The PEGMA segments could produce hydrophilic domains formed on the interface so as to achieve stable electroosmotic flow, and less nonspecific adsorption toward biomolecules. The modification procedure and the properties of the poly(BMA-co-PEGMA)-coated surface have been characterized by FT-IR spectroscopy, confocal fluorescence microscopy, X-ray photoelectron spectroscopy and scanning electron microscopy. The water contact angle and electroosmotic flow of PEG-modified PMMA microchip are measured to be 36 degrees and 5.4 x 10(-4) cm(2) V(-1) s(-1), while those of 73 degrees and 1.9 x 10(-4) cm(2) V(-1) s(-1) for native one, respectively. The PEG-modified microchip has been applied for the electrophoresis separation of proteins, corresponding to the theoretical efficiencies about 16 300 and 412 300 plates m(-1). In the interest of achieving efficient separation while minimizing biofoulings from the serum and plasma, the fabrication of PEG-coated microfluidic chips would provide a biocompatible platform for complex biological analysis.