scholarly journals Mass Spectrometry-Guided Optimization and Characterization of a Biologically Active Transferrin–Lysozyme Model Drug Conjugate

2013 ◽  
Vol 10 (5) ◽  
pp. 1998-2007 ◽  
Author(s):  
Son N. Nguyen ◽  
Cedric E. Bobst ◽  
Igor A. Kaltashov
Keyword(s):  
Mass Spectrometry ◽  
Biologically Active ◽  
Drug Conjugate ◽  
Model Drug

scholarly journals Native mass spectrometry and ion mobility characterization of trastuzumab emtansine, a lysine-linked antibody drug conjugate

2015 ◽  
Vol 24 (8) ◽  
pp. 1210-1223 ◽  
Author(s):  
Julien Marcoux ◽  
Thierry Champion ◽  
Olivier Colas ◽  
Elsa Wagner-Rousset ◽  
Nathalie Corvaïa ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Ion Mobility ◽  
Native Mass Spectrometry ◽  
Trastuzumab Emtansine ◽  
Antibody Drug Conjugate ◽  
Drug Conjugate ◽  
Antibody Drug

Characterization of the selected honeybee products based on omics techniques

2019 ◽  
Vol 88 (2) ◽  
pp. 129-132
Author(s):  
Eliza Matuszewska ◽  
Paweł Dereziński ◽  
Agnieszka Klupczyńska ◽  
Agata Światły-Błaszkiewicz ◽  
Szymon Plewa ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Dietary Supplements ◽  
Royal Jelly ◽  
Biologically Active ◽  
Human Organism ◽  
Pharmacological Properties ◽  
Bioactive Components ◽  
Honeybee Venom ◽  
Harmful Effects

to comprehensively characterize honeybee venom, royal jelly, propolis, and pollen, by applying advanced analytical and bioinformatics methodologies. Honeybee products (HBP) contain many bioactive components with both beneficial and harmful effects on the human organism. Nevertheless, the overall composition of the HBP remains not fully investigated. Thus, this research is focused on complementary proteomic and metabolomic characterization of biologically active compounds derived from HBP, regarding their toxicological and pharmacological properties. The objectives of the study will be achieved by the application of up to date mass spectrometry techniques. Due to increasing interest in using of HBP in medicine, this project will contribute to improving the safety of HBP‑derived dietary supplements and drugs.

Towards the Standard-Module Approach to Disulfide-Linked Polypeptide Nanostructures. I. Methodological Prerequisites and Mass Spectrometric Characterization of the Test Two-Loop Structure

2003 ◽  
Vol 9 (2) ◽  
pp. 139-148 ◽  
Author(s):  
O.A. Mirgorodskaya ◽  
K.F. Haselmann ◽  
F. Kjeldsen ◽  
R.A. Zubarev ◽  
P. Roepstorff
Keyword(s):  
Mass Spectrometry ◽  
Disulfide Bonds ◽  
Bond Cleavage ◽  
Bond Formation ◽  
Peptide Bond ◽  
Biologically Active ◽  
Loop Structure ◽  
Partial Acid Hydrolysis ◽  
Peptide Bond Cleavage

Potentially biologically-active nanostructures can be created from single chains of unmodified peptides by cross-linking different regions of the chain by disulfide bonds and cleaving the chain at specified sites to obtain the final configuration. The availability of techniques for assembly and characterization of such structures was tested on a two-loop structure created from a 21-residue linear peptide. Directed intra-molecular disulfide bond formation was performed by inserting partial sequences favoring intra-molecular S–S bond formation (“loops”) separated by partial sequences disfavoring such a process (“spacers”) into the precursor sequence. Peptide bond cleavage by partial acid hydrolysis at specific sites (GG, NP/DP) inside the loops opened them; the same process in the spacer separated the loops. Synthesis, oxidation and bond cleavage were monitored by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI ToF MS). The hydrolysis fragments of the produced nanostructures were characterized by tandem electrospray ionization Fourier transform mass spectrometry (ESI FT-MS) with collisional and electron capture dissociations. The latter technique was especially useful as it cleaves S–S bonds preferentially. The feasibility of the proposed synthesis approach and the adequacy of the analysis techniques for the test structure were demonstrated.

scholarly journals Correction to Comprehensive Middle-Down Mass Spectrometry Characterization of an Antibody–Drug Conjugate by Combined Ion Activation Methods

2020 ◽  
Vol 92 (17) ◽  
pp. 12097-12097
Author(s):  
Eleanor Watts ◽  
Jon D. Williams ◽  
Laura J. Miesbauer ◽  
Milan Bruncko ◽  
Jennifer S. Brodbelt
Keyword(s):  
Mass Spectrometry ◽  
Antibody Drug Conjugate ◽  
Ion Activation ◽  
Drug Conjugate ◽  
Antibody Drug

Characterization of the 12% trichloroacetic acid-insoluble oligopeptides of Parmigiano-Reggiano cheese

1992 ◽  
Vol 59 (3) ◽  
pp. 401-411 ◽  
Author(s):  
Francesco Addeo ◽  
Lina Chianese ◽  
Antonio Salzano ◽  
Raffaele Sacchi ◽  
Ugo Cappuccio ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Molecular Mass ◽  
Trichloroacetic Acid ◽  
Fast Atom Bombardment ◽  
Biologically Active ◽  
Isolation And Identification ◽  
Chemical Methods ◽  
Parmigiano Reggiano

SummaryThe isolation and identification of low molecular mass peptides formed during the ripening of Parmigiano-Reggiano cheese is described. A strategy was used based on the fractionation of nitrogenous material using chemical methods followed by HPLC to isolate peptides and fast atom bombardment-mass spectrometry to identify them. It was found that the majority of cheese oligopeptides arose from the proteolysis of β-casein. Several phosphopeptides and oligopeptides known in vivo to be biologically active have also been identified during the ripening of cheese.

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