ABSTRACT
Quantitative analysis of red phosphorus in polypropylene was studied using a temperature programmable pyrolyzer in combination with a mass spectrometer. Evolved gas analysis (EGA) profiles were obtained by continuous measurements of evolved gases from a sample while heating the sample at a constant heating rate. During heating of the sample, red phosphorus sublimates into P4 molecules, which have characteristic ions (m/z 31, 62, 93 and 124). Red phosphorus in polypropylene was determined from the m/z 62 ion peak area of the EGA profile with good reproducibility. The determined value was close to the value of original formulation and to the one determined by pyrolysis-GC/MS.
ABSTRACT
This study aims to quantitatively investigate the interaction between sulfated polysaccharides with potent anti-HIV activity, dextran and curdlan sulfates with negatively charged sulfate groups, and poly-L-lysine as a model protein and oligopeptides from a HIV surface glycoprotein gp120 with positively charged amino acids using surface plasmon resonance (SPR) and dynamic light scattering (DLS) to elucidate the anti-HIV mechanism of sulfated polysaccharides. The apparent association- (ka) and dissociation rate (kd) constants of dextran and curdlan sulfates against poly-L-lysine were kaâ¯=â¯6.92â¯×â¯104-2.17â¯×â¯106â¯1/Ms and kdâ¯=â¯4.29â¯×â¯10-5-2.22â¯×â¯10-4â¯1/s; these kinetic constants were dependent on the molecular weights and degree of sulfation of sulfated polysaccharides. For interaction, the three oligopeptides from the HIV gp120 were peptide A 297TRPNNNTRKRIRIQRGPGRA316 with several lysine (K) and arginine (R) in the V3 loop region, peptide B 493PLGVAPTKAKRRVVQREKR511 with several K and R in the C-terminus region, and oligopeptide C 362KQSSGGDPEIVTHSFNCGG380 with few basic amino acids in the CD4 binding domain. Sulfated polysaccharides exhibited strong interaction against oligopeptides A and B, (kaâ¯=â¯5.48â¯×â¯104-2.96â¯×â¯106â¯1/Ms. and kdâ¯=â¯1.74â¯×â¯10-4-6.24â¯×â¯10-3â¯1/s), no interaction was noted against oligopeptide C. Moreover, the particle size and zeta potential by DLS indicated the interaction between sulfated polysaccharides and oligopeptides A and B, suggesting the anti-HIV mechanism of sulfated polysaccharides to be the electrostatic interaction of negatively charged sulfated polysaccharides and HIV at the positively charged amino acid regions.