Self-Similar Tilings of Fractal Blow-Ups

New tilings of certain subsets of $\mathbb{R}^{M}$ are studied, tilings associated with fractal blow-ups of certain similitude iterated function systems (IFS). For each such IFS with attractor satisfying the open set condition, our construction produces a usually infinite family of tilings that satisfy the following properties: (1) the prototile set is finite; (2) the tilings are repetitive (quasiperiodic); (3) each family contains self-similartilings, usually infinitely many; and (4) when the IFS is rigid in an appropriate sense, the tiling has no non-trivial symmetry; in particular the tiling is non-periodic

Synthesis route of dehydroabietyltrimethyl ammonium bromine.

<p>Synthesis route of dehydroabietyltrimethyl ammonium bromine.</p

FTIR spectra of surfactant, as-synthesized and calcined supermicroporous titanias.

<p>FTIR spectra of surfactant, as-synthesized and calcined supermicroporous titanias.</p

Quantitation of Site-Specific Glycosylation in Manufactured Recombinant Monoclonal Antibody Drugs

During the development of recombinant monoclonal antibody (rMAb) drugs, glycosylation receives particular focus because changes in the attached glycans can have a significant impact on the antibody effector functions. The vast heterogeneity of structures that exist across glycosylation sites hinders the in-depth analysis of glycan changes specific to an individual protein within a complex mixture. In this study, we established a sensitive and specific method for monitoring site-specific glycosylation in rMAbs using multiple reaction monitoring (MRM) on an ultrahigh-performance liquid chromatography–triple quadrupole MS (UHPLC-QqQ-MS). Our results showed that irrespective of the IgG subclass expressed in the drugs, the N-glycopeptide profiles are nearly the same but differ in abundances. In all rMAb drugs, a single subclass of IgG comprised over 97% of the total IgG content and showed over 97% N-glycan site occupancy. This study demonstrates the utility of an MRM-based method to rapidly characterize over 130 distinct glycopeptides and determine the extent of site occupancy within minutes. Such multilevel structural characterization is important for the successful development of therapeutic antibodies