4.6 Article

Oxidation of specific tryptophan residues inhibits high-affinity binding of cocaine and its metabolites to a humanized anticocaine mAb

相关参考文献

注意:仅列出部分参考文献,下载原文获取全部文献信息。
Article Biochemistry & Molecular Biology

Ligand binding to a humanized anti-cocaine mAb measured by dye absorption spectroscopy

Terence L. Kirley et al.

Summary: A novel technique using absorption spectroscopy and fluorescence is demonstrated to directly evaluate the antigen binding function of therapeutic mAb in their formulation buffers, as well as qualitatively assess the relative affinities of various metabolites. Data obtained from these assays confirm the proper function of the therapeutic product and show differential effects of conditions like pH on metabolite binding capacity.

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS (2021)

Article Biochemistry & Molecular Biology

Monoclonal Antibody Aggregation Associated with Free Radical Induced Oxidation

Kai Zheng et al.

Summary: Oxidation is a key degradation pathway for protein drugs, which can impact product efficacy and patient safety. This study found that oxidation led to the oxidation of methionine and tryptophan residues, as well as increased protein aggregation. Excipients such as tryptophan, pyridoxine, or tyrosine were shown to effectively reduce protein aggregation induced by oxidative stress.

INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES (2021)

Article Biochemical Research Methods

Cocaine binding to the Fab fragment of a humanized anti-cocaine mAb quantitated by dye absorption and fluorescence spectroscopy

Terence L. Kirley et al.

Summary: In this study, we demonstrate a simple and inexpensive method for quantitating cocaine binding to a recombinant humanized anti-cocaine antibody Fab fragment using absorption and fluorescence measurements with DASPMI and SYPRO Orange dyes. We found that the effect of cocaine binding on dye absorbance differed greatly between the intact antibody and the Fab fragment, with a significant decrease in dye absorbance for the Fab fragment. This technique can also distinguish between high and low affinity cocaine metabolites, making it useful for evaluating Fab fragment suitability for in vivo use and other biochemical assessments.

JOURNAL OF IMMUNOLOGICAL METHODS (2021)

Article Biochemical Research Methods

A novel differential scanning fluorimetry analysis of a humanized anticocaine mAb and its ligand binding characteristics

Terence L. Kirley et al.

JOURNAL OF IMMUNOLOGICAL METHODS (2020)

Article Biochemical Research Methods

Structural analysis of free and liganded forms of the Fab fragment of a high-affinity anti-cocaine antibody, h2E2

Kemin Tan et al.

ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS (2019)

Article Biochemistry & Molecular Biology

Unfolding of IgG domains detected by non-reducing SDS-PAGE

Terence L. Kirley et al.

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS (2018)

Article Biochemistry & Molecular Biology

Characterization of a recombinant humanized anti-cocaine monoclonal antibody produced from multiple clones for the selection of a master cell bank candidate

Hanna N. Wetzel et al.

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS (2017)

Article Chemistry, Medicinal

Selective Oxidation of Methionine and Tryptophan Residues in a Therapeutic IgG1 Molecule

Emilien Folzer et al.

JOURNAL OF PHARMACEUTICAL SCIENCES (2015)

Article Biotechnology & Applied Microbiology

Characterization of a recombinant humanized anti-cocaine monoclonal antibody and its Fab fragment

Terence L. Kirley et al.

HUMAN VACCINES & IMMUNOTHERAPEUTICS (2015)

Article Pharmacology & Pharmacy

A Recombinant Humanized Anti-Cocaine Monoclonal Antibody Inhibits the Distribution of Cocaine to the Brain in Rats

Andrew B. Norman et al.

DRUG METABOLISM AND DISPOSITION (2014)

Review Pharmacology & Pharmacy

Medications development: Successes and challenges

F Vocci et al.

PHARMACOLOGY & THERAPEUTICS (2005)