Academic Journal

Structural Investigation of Therapeutic Antibodies Using Hydroxyl Radical Protein Footprinting Methods

التفاصيل البيبلوغرافية
العنوان: Structural Investigation of Therapeutic Antibodies Using Hydroxyl Radical Protein Footprinting Methods
المؤلفون: Corie Y. Ralston, Joshua S. Sharp
المصدر: Antibodies; Volume 11; Issue 4; Pages: 71
بيانات النشر: Multidisciplinary Digital Publishing Institute
سنة النشر: 2022
المجموعة: MDPI Open Access Publishing
مصطلحات موضوعية: hydroxyl radical footprinting, structural mass spectrometry, fast photochemical oxidation of proteins (FPOP), flash oxidation (FOX), X-ray footprinting with mass spectrometry (XFMS), therapeutic antibody structure
الوصف: Commercial monoclonal antibodies are growing and important components of modern therapies against a multitude of human diseases. Well-known high-resolution structural methods such as protein crystallography are often used to characterize antibody structures and to determine paratope and/or epitope binding regions in order to refine antibody design. However, many standard structural techniques require specialized sample preparation that may perturb antibody structure or require high concentrations or other conditions that are far from the conditions conducive to the accurate determination of antigen binding or kinetics. We describe here in this minireview the relatively new method of hydroxyl radical protein footprinting, a solution-state method that can provide structural and kinetic information on antibodies or antibody–antigen interactions useful for therapeutic antibody design. We provide a brief history of hydroxyl radical footprinting, examples of current implementations, and recent advances in throughput and accessibility.
نوع الوثيقة: text
وصف الملف: application/pdf
اللغة: English
Relation: https://dx.doi.org/10.3390/antib11040071
DOI: 10.3390/antib11040071
الاتاحة: https://doi.org/10.3390/antib11040071
Rights: https://creativecommons.org/licenses/by/4.0/
رقم الانضمام: edsbas.EC53A808
قاعدة البيانات: BASE