SavedAdd your journal

Journals / Turkish Journal of Biology / 2019 / Cilt: 43 - Sayı: 1

Protein engineering approaches for antibody fragments: directed evolution and rational design approaches

Sibel KALYONCU
Merve ARSLAN
Dilara KARADAĞ
Pages
1–12
Publication Date
2022-10-18
DOI
—
🏛️Bibliographic metadata and full text access for this article are provided via DergiPark.
DergiPark Record ↗
✨

AI Summary & Key Takeaways

AI Insight
⚡ TL;DR(Too Long; Didn't Read)

Recent developments in rationaldesign approaches and antibody display technologies, and especially phage display, which was recently awarded the 2018 Nobel Prize,are discussed to be used in antibody research and development.

📌 3 Key Takeaways

🎯
Objective & Hypothesis:The number of therapeutic antibodies in preclinical, clinical, or approved phases has been increasing exponentially, mostlydue to their known successes.
📊
Key Findings & Data:Development of antibody engineering methods has substantially hastened the development of therapeuticantibodies.
💡
Conclusion & Impact:Recent developments in rationaldesign approaches and antibody display technologies, and especially phage display, which was recently awarded the 2018 Nobel Prize,are discussed to be used in antibody research and development.
🔬Design:Review & Systematic Survey
📍Scope:2018 Verileri
⚙️Variables:Domain Parameters

Abstract

The number of therapeutic antibodies in preclinical, clinical, or approved phases has been increasing exponentially, mostlydue to their known successes. Development of antibody engineering methods has substantially hastened the development of therapeuticantibodies. A variety of protein engineering techniques can be applied to antibodies to improve their affinity and/or biophysical propertiessuch as solubility and stability. Antibody fragments (where all or some parts of constant regions are eliminated while the essentialantigen binding region is preserved) are more suitable for protein engineering techniques because there are many in vitro screeningtechnologies available for antibody fragments but not full-length antibodies. Improvement of biophysical characteristics is importantin the early development phase because most antibodies fail at the later stage of development and this leads to loss of resources andtime. Here, we review directed evolution and rational design methods to improve antibody properties. Recent developments in rationaldesign approaches and antibody display technologies, and especially phage display, which was recently awarded the 2018 Nobel Prize,are discussed to be used in antibody research and development.

🔖

Cite This Article

KALYONCU, S., ARSLAN, M., KARADAĞ, D. (2022). Protein engineering approaches for antibody fragments: directed evolution and rational design approaches. Turkish Journal of Biology, Cilt: 43 - Sayı: 1, 1–12. https://ajindex.com/articles/600230

📄 Full Text PDF Viewer

📄

PDF görüntüleyici hazırlanıyor...

References (11)

  1. Agrawal NJ, Kumar S, Wang XL, Helk, B, Singh SK, Trout BL (2011). Aggregation in protein-based biotherapeutics: computational studies and tools to identify aggregation-prone Regions. Journal of Pharmaceutical Sciences 100: 5081-5095.
  2. Bain B, Brazil M (2003). Adalimumab. Nature Reviews Drug Discovery 2: 693-694.
  3. Bava KA, Gromiha MM, Uedaira H, Kitajima K, Sarai A (2004). ProTherm, version 4.0: thermodynamic database for proteins and mutants. Nucleic Acids Research 32: D120-D121. Beerten J, Van Durme J, Gallardo R, Capriotti E, Serpell L, Rousseau F, Schymkowitz J (2015). WALTZ-DB: a benchmark database of amyloidogenic hexapeptides. Bioinformatics 31: 1698-1700.
  4. Bradbury A, Pluckthun A (2015). Standardize antibodies used in research. Nature 518: 27-29.
  5. Brodel AK, Isalan M, Jaramillo A (2018). Engineering of biomolecules by bacteriophage directed evolution. Current Opinion in Biotechnology 51: 32-38.
  6. Capriotti E, Fariselli P, Casadio R (2004). A neural-network-based method for predicting protein stability changes upon single point mutations. Bioinformatics 20: 63-68.
  7. Capriotti E, Fariselli P, Casadio R (2005). I-Mutant2.0: predicting stability changes upon mutation from the protein sequence or structure. Nucleic Acids Research 33: W306-W310. Chan CE, Lim AP, MacAry PA, Hanson BJ (2014). The role of phage display in therapeutic antibody discovery. International Immunology 26: 649-657.
  8. Chao G, Lau W L, Hackel BJ, Sazinsky SL, Lippow SM, Wittrup KD (2006). Isolating and engineering human antibodies using yeast surface display. Nature Protocols 1: 755-768.
  9. Cheng JL, Randall A, Baldi P (2006). Prediction of protein stability changes for single-site mutations using support vector machines. Proteins-Structure Function and Bioinformatics 62: 1125-1132.
  10. Chiu ML, Gilliland GL (2016). Engineering antibody therapeutics. Current Opinion in Structural Biology 38: 163-173. Conchillo-Sole O, de Groot NS, Aviles FX, Vendrell J, Daura X, Ventura S (2007). AGGRESCAN: a server for the prediction and evaluation of “hot spots” of aggregation in polypeptides. BMC Bioinformatics 8: 65. Courtois F, Agrawal NJ, Lauer TM, Trout BL (2016). Rational design of therapeutic mAbs against aggregation through protein engineering and incorporation of glycosylation motifs applied to bevacizumab. MAbs 8: 99-112.
  11. Dubay KF, Pawar AP, Chiti F, Zurdo J, Dobson CM, Vendruscolo M (2004). Prediction of the absolute aggregation rates of amyloidogenic polypeptide chains. Journal of Molecular Biology 341: