scholarly journals An odor delivery system for arbitrary time-varying patterns of odors, mixtures and concentrations

2016 ◽  
Author(s):  
Priyanka Gupta ◽  
Dinu F Albeanu ◽  
Upinder S Bhalla
Keyword(s):  
Delivery System ◽  
Single Pulse ◽  
Local Environment ◽  
Ternary Mixtures ◽  
Time Varying ◽  
Arbitrary Time ◽  
Long Duration ◽  
Odor Plumes ◽  
Individual Odors

AbstractOdor stimuli in the natural environment are intermittent and the concentration of any given odor fluctuates rapidly over time. Further, even in the simplest scenario, the olfactory sensors receive uncorrelated, intermittent inputs in the form of odor plumes arising from several odor sources in the local environment. However, typically used odor stimuli under laboratory settings are restricted to long-duration (~seconds), single pulse of one odor at a time that are rarely encountered in nature. This inadequate choice of odor stimuli is due to the dearth of affordable odor delivery systems that can generate plume-like, naturalistic stimuli with high reproducibility such as to allow for repeat measurements under laboratory conditions. We thus developed an odor delivery system that generates arbitrary time-varying patterns of individual odors and ternary mixtures at time scales of ~20 Hz. Here, we provide a detailed description of the construction and output characterization of our odor delivery system.

scholarly journals Development and Characterization of PLGA‐Based Multistage Delivery System for Enhanced Payload Delivery to Targeted Vascular Endothelium

2021 ◽  
pp. 2000377
Author(s):  
Jorge A. Palma‐Chavez ◽  
Kevin Fuentes ◽  
Brian E. Applegate ◽  
Javier A. Jo ◽  
Phapanin Charoenphol
Keyword(s):  
Delivery System ◽  
Vascular Endothelium

scholarly journals Size-based characterization of adalimumab and TNF-α interactions using flow induced dispersion analysis: assessment of avidity-stabilized multiple bound species

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Morten E. Pedersen ◽  
Ragna M. S. Haegebaert ◽  
Jesper Østergaard ◽  
Henrik Jensen
Keyword(s):  
Protein Interactions ◽  
Free Ligand ◽  
Local Environment ◽  
Dispersion Analysis ◽  
Surface Immobilization ◽  
Covalent Bonds ◽  
Essential Information ◽  
Tnf Α

AbstractThe understanding and characterization of protein interactions is crucial for elucidation of complicated biomolecular processes as well as for the development of new biopharmaceutical therapies. Often, protein interactions involve multiple binding, avidity, oligomerization, and are dependent on the local environment. Current analytical methodologies are unable to provide a detailed mechanistic characterization considering all these parameters, since they often rely on surface immobilization, cannot measure under biorelevant conditions, or do not feature a structurally-related readout for indicating formation of multiple bound species. In this work, we report the use of flow induced dispersion analysis (FIDA) for in-solution characterization of complex protein interactions under in vivo like conditions. FIDA is an immobilization-free ligand binding methodology employing Taylor dispersion analysis for measuring the hydrodynamic radius (size) of biomolecular complexes. Here, the FIDA technology is utilized for a size-based characterization of the interaction between TNF-α and adalimumab. We report concentration-dependent complex sizes, binding affinities (Kd), kinetics, and higher order stoichiometries, thus providing essential information on the TNF-α–adalimumab binding mechanism. Furthermore, it is shown that the avidity stabilized complexes involving formation of multiple non-covalent bonds are formed on a longer timescale than the primary complexes formed in a simple 1 to 1 binding event.

Sign in / Sign up

Export Citation Format

Share Document