Supramolecular Organization Predicts Protein Nanoparticle Delivery to Neutrophils for Acute Lung Inflammation Diagnosis and Treatment

Jacob W. Myerson; Priyal N. Patel; Nahal Habibi; Landis R. Walsh; Yi-Wei Lee; David C. Luther; Laura T. Ferguson; Michael H. Zaleski; Marco E. Zamora; Oscar A. Marcos-Contreras; Patrick M. Glassman; Ian Johnston; Elizabeth D. Hood; Tea Shuvaeva; Jason V. Gregory; Raisa Y. Kiseleva; Jia Nong; Kathryn M. Rubey; Colin F. Greineder; Samir Mitragotri; George S. Worthen; Vincent M. Rotello; Joerg Lahann; Vladimir R. Muzykantov; Jacob S. Brenner

Indeed, CD spectroscopic and ANSA structural characterization of DBCOmodified IgG and DBCO-IgG liposomes resembled results obtained for LDNGs and crosslinked albumin NPs. IgG secondary structure, as assessed by CD spectroscopy, was unchanged by DBCO modification (Supplementary Figure 19A) . Deconvolution of CD spectra via neural network algorithm indicated identical structural compositions for . CC-BY-NC-ND 4.0 International license author/funder. It is made available under a The copyright holder for this preprint (which was not peer-reviewed) is the . https://doi.org/10.1101/2020.04.15.037564 doi: bioRxiv preprint DBCO(20X)-IgG, DBCO(10X)-IgG, DBCO(5X)-IgG, DBCO(2.5X)-IgG, and unmodified IgG, showing that IgG was not denatured by conjugation to DBCO. ANSA was used to probe accessible hydrophobic domains on DBCO(20X)-IgG and DBCO(20X)-IgG liposomes (Supplementary Figure 19B) . ANSA fluorescence indicated more hydrophobic domains available on DBCO(20X)-IgG liposomes than on DBCO(20X)-IgG itself, resembling results for lysozyme and LDNGs.