Geranyl pyrophosphate synthase: Characterization of the enzyme and evidence that this chain-length specific prenyltransferase is associated with monoterpene biosynthesis in sage (Salvia officinalis)

1989 ◽  
Vol 271 (2) ◽  
pp. 524-535 ◽  
Author(s):  
Rodney Croteau ◽  
Paul T. Purkett
2012 ◽  
Vol 3 ◽  
pp. 12-24 ◽  
Author(s):  
Hicham Hamoudi ◽  
Ping Kao ◽  
Alexei Nefedov ◽  
David L Allara ◽  
Michael Zharnikov

Self-assembled monolayers (SAMs) of nitrile-substituted oligo(phenylene ethynylene) thiols (NC-OPEn) with a variable chain length n (n ranging from one to three structural units) on Au(111) were studied by synchrotron-based high-resolution X-ray photoelectron spectroscopy and near-edge absorption fine-structure spectroscopy. The experimental data suggest that the NC-OPEn molecules form well-defined SAMs on Au(111), with all the molecules bound to the substrate through the gold–thiolate anchor and the nitrile tail groups located at the SAM–ambient interface. The packing density in these SAMs was found to be close to that of alkanethiolate monolayers on Au(111), independent of the chain length. Similar behavior was found for the molecular inclination, with an average tilt angle of ~33–36° for all the target systems. In contrast, the average twist of the OPEn backbone (planar conformation) was found to depend on the molecular length, being close to 45° for the films comprising the short OPE chains and ~53.5° for the long chains. Analysis of the data suggests that the attachment of the nitrile moiety, which served as a spectroscopic marker group, to the OPEn backbone did not significantly affect the molecular orientation in the SAMs.


2010 ◽  
Vol 29 (8) ◽  
pp. 966-971 ◽  
Author(s):  
Sylvain Chardron ◽  
Stéphane Bruzaud ◽  
Brigitte Lignot ◽  
Anne Elain ◽  
Olivier Sire

2019 ◽  
Vol 20 (21) ◽  
pp. 5426
Author(s):  
Stephan Harm ◽  
Karl Lohner ◽  
Ute Fichtinger ◽  
Claudia Schildböck ◽  
Jennifer Zottl ◽  
...  

Acylation of antimicrobial peptides mimics the structure of the natural lipopeptide polymyxin B, and increases antimicrobial and endotoxin-neutralizing activities. In this study, the antimicrobial properties of lactoferrin-based LF11 peptides as well as blood compatibility as a function of acyl chain length were investigated. Beyond the classical hemolysis test, the biocompatibility was determined with human leukocytes and platelets, and the influence of antimicrobial peptides (AMPs) on the plasmatic coagulation and the complement system was investigated. The results of this study show that the acylation of cationic peptides significantly reduces blood tolerance. With increasing acyl chain length, the cytotoxicity of LF11 peptides to human blood cells also increased. This study also shows that acylated cationic antimicrobial peptides are inactivated by the presence of heparin. In addition, it could be shown that the immobilization of LF11 peptides leads to a loss of their antimicrobial properties.


e-Polymers ◽  
2006 ◽  
Vol 6 (1) ◽  
Author(s):  
J. L. Feng ◽  
C. Y. Yue ◽  
K. S. Chian

AbstractThis project aims to develop and characterize a series of bismaleimide (BMI) polymers based on maleic anhydride and aliphatic-ether diamines. The effects of varying the chain length of aliphatic-ether diamines on the resultant bismaleimide systems were evaluated so that their suitability for microelectronics applications could be evaluated. The synthetic reaction and properties of the bismaleimide materials were investigated using Fourier Transform Infrared Spectroscopy (FTIR), Differential Scanning Calorimetry (DSC), Thermo- Gravimetric Analysis (TGA), Dielectric Thermal Analysis (DEA) and rheometry. Results showed that thermal, dielectric and rheological properties were all affected by the main chain length of BMI. The magnitude of the dielectric constant at 100 kHz increases with the increasing chain length. The curing peak temperature, curing heat and degradation temperature of BMI, all decrease with the increasing chain length.


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