Hybrid Coatings of SiO2-Recycled PET Unsaturated Polyester Resin by Sol-Gel Process.

Hybrid coatings of SiO2 and recycled unsaturated polyester resin (R-UPR) from recycled polyethylene-terephthalate (PET) were prepared by the sol-gel process on glass substrates. First, SiO2 was synthesized by the sol-gel process using a tetraethyl orthosilicate (TEOS) solution. Next, bis(2-hydroxypropyl-terephthalate) (BHPT) was synthesized from mechanical and chemical recycling (glycolysis) of post-consumer PET bottles in propylene glycol (PG) using ZnA as catalyst, in a Vessel-type reactor (20-200 °C); maleic anhydride (MA) was added and, following the same procedure, the unsaturated polyester (UP) was synthetized, which was cooled to room temperature. Next, styrene (St) and benzoyl-peroxide (PBO)-initiator were added to obtain R-UPR. TEOS (T) and three hybrid solutions were synthesized, with molar ratios of 0:1:0 (T), 1:2:0.25 (H1), 1:1:0.25 (H2), and 1:0:0.25 (H3) for R-UPR:TEOS:3-trimethoxy-(silyl)-propyl-methacrylate (TMSPM), respectively, with which TC, HC1, HC2, and HC3 coatings were elaborated using the immersion technique and polymerized (120 °C for 24 h). The solutions were characterized by FT-IR and TGA, and the coatings by SEM, nanoindentation, AFM, adhesion, and contact angle. The results showed that SiO2 enhanced mechanical (hardness and Young's modulus) and thermal properties of the R-UPR. The coatings adhered perfectly to the substrate, with thicknesses of micrometer units and a flat surface; in addition, hydrophilicity decreased as SiO2 decreased.

How FMN binds to anabaena apoflavodoxin: a hydrophobic encounter at an open binding site.

Molecular recognition begins when two molecules approach and establish interactions of certain strength. The mechanisms of molecular recognition reactions between biological molecules are not well known, and few systems have been analyzed in detail. We investigate here the reaction between an apoprotein and its physiological cofactor (apoflavodoxin and flavin mononucleotide) that binds reversibly to form a non-covalent complex (flavodoxin) involved in electron transfer reactions. We have analyzed the fast binding reactions between the FMN cofactor (and shorter analogs) and wild type (and nine mutant apoflavodoxins where residues interacting with FMN in the final complex have been replaced). The x-ray structures of two such mutants are reported that show the mutations are well tolerated by the protein. From the calculated microscopic binding rate constants we have performed a Phi analysis of the transition state of complex formation that indicates that the binding starts by interaction of the isoalloxazine-fused rings in FMN with residues of its hydrophobic binding site. In contrast, the phosphate in FMN, known to contribute most to the affinity of the final holoflavodoxin complex, is not bound in the transition state complex. Both the effects of ionic strength and of phosphate concentration on the wild type complex rate constant agree with this scenario. As suggested previously by nmr data, it seems that the isoalloxazine-binding site may be substantially open in solution. Interestingly, although FMN is a charged molecule, electrostatic interactions seem not to play a role in directing the binding, unlike what has been reported for other biological complexes. The binding can thus be best described as a hydrophobic encounter at an open binding site.

Expression, crystallization and preliminary X-ray diffraction studies on the complete choline-binding domain of the major pneumococcal autolysin.

The major pneumococcal autolysin (LytA), a virulence factor of this bacterium, is composed of an amino-terminal catalytic domain plus a carboxyl-terminal choline-binding domain (ChBD). This C-terminal domain, responsible for anchorage to the cell wall, is a tandem of six imperfect 20-residue repeats whose precise ends have been difficult to establish by sequence methods. The reported crystal structure of a shortened C-terminal fragment of the protein suggested that it might contain an additional repeat and thus an additional choline-binding site (ChBS). The complete recombinant choline-binding domain of LytA has now been overexpressed in soluble form using a secreting Escherichia coli strain which facilitates purification with a higher yield. It has been crystallized at room temperature using MPD as the main precipitant. The crystals belong to space group P2(1) and diffract to beyond 3.2 A resolution on a synchrotron-radiation source. The molecular-replacement solution indicates that a new ChBS which fits the topology of the solenoid structure is formed in the N-terminal region.