Momenta Pharmaceuticals, Inc.

Janssen Biotech, Inc.

Jonathan C Lansing

Carlos J Bosques

Daniel Ortiz

Laura Rutitzky

Zachary Shriver

James S Huston

James Meador, Iii

Leona E Ling

Daniela Beccati

Ian Christopher Parsons

Xiangping Zhu

Corinne Bauer

Yanjie Jiang

Cuihua Liu

Xiao-Jin Xu

Shiming Dong

Nathaniel J Washburn

Ganesh Kaundinya

Scott Bailey

Ganesh Venkataraman

Ishan Capila

Birgit Corinna Schultes

Naveen Bhatnagar

Hetal Sarvaiya

Daniela Becatti

Robin Meccariello

Nathanial J Washburn

Brigit C Schultes

The present invention relates to methods of using biologically active Fc domain-containing therapeutic constructs (Fc constructs) to induce immune cell activation of the immune response in a subject, and for example, to treat diseases such as cancers and infections in a subject. Such Fc constructs may include 5 or more Fc domains.

Methods related to engineered Fc constructs

The present disclosure relates to engineered IgG Fc constructs and uses thereof.

Compositions and methods related to engineered Fc constructs

The present invention relates to compositions and methods of engineered IgG Fc constructs, wherein said Fc constructs include one or more Fc domains.

Engineered Fc constructs

The present disclosure relates to compositions and methods of engineered IgG Fc constructs, wherein the Fc constructs include one or more Fc domains.

The present invention relates to engineered IgG Fc constructs and uses thereof.

The present disclosure provides a method for determining the relative conformations of a protein provided in different protein preparations, comprising steps of: (i) obtaining a first 2D NOESY NMR spectrum of a first protein preparation; (ii) obtaining a second 2D NOESY NMR spectrum of a second protein preparation; and (iii); determining whether a protein has a different conformation in the first and second protein preparations by comparing one or more cross-peaks in the first 2D NOESY NMR spectrum with one or more corresponding cross-peaks in the second 2D NOESY NMR spectrum.

Comparative analysis of protein conformations by using 2D NOESY NMR spectra

The presently disclosed subject matter provides methods for evaluating and characterizing peptides, peptide mixtures, and polypeptide mixtures. More particularly, the presently disclosed subject matter provides methods for evaluating or characterizing complex peptide or polypeptide mixtures comprising glutamic acid, alanine, tyrosine, and lysine, e.g., Copolymer-1 or glatiramer acetate, including, but not limited to, methods of identifying, isolating, quantifying, and purifying amino acids, peptides, polypeptides, and combinations thereof having a diethylamide group instead of a carboxyl group present on the C-terminus. The presently disclosed methods can be used to determine the mole percent of polypeptides having a diethylamide group at a C-terminus thereof and can be used to evaluate one or more properties of a sample of one polypeptide mixture as compared to one or more properties of a different sample of a polypeptide mixture.

Methods of evaluating peptide mixtures

Methods of evaluating diethylamide in peptide mixtures for the preparation of glatiramer acetate

Methods of analyzing glatiramer acetate (GA) or a polymeric precursor thereof are provided. The methods can include determining a level of one or more diethylamide-modified amino acids in a sample comprising GA or a polymeric precursor thereof, and selecting at least a portion of the sample based on the assessment of the one or more diethylamide-modified amino acids in the sample.

Evaluation of copolymer diethylamide

The present disclosure provides nuclear magnetic resonance (NMR) methods for characterizing mixtures of N-linked glycans. Without limitation, methods of the present disclosure may be useful in characterizing monosaccharide composition, branching, fucosylation, sulfation, phosphorylation, sialylation linkages, presence of impurities and/or efficiency of a labeling procedure (e.g., labeling with a fluorophore such as 2-AB). In certain embodiments, the methods can be used quantitatively. In certain embodiments, the methods can be combined with enzymatic digestion to further characterize glycan mixtures.

Characterization of N-glycan mixtures by nuclear magnetic resonance

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Reading, MA, United States of America

Jonathan C Lansing