Chemical Synthesis of the Highly Hydrophobic Antiviral Membrane-Associated Protein IFITM3 and Modified Variants

Autor: Vijaya R. Pattabiraman, Jeffrey W. Bode, Thibault J. Harmand
Rok vydání: 2017
Předmět:
0301 basic medicine
Models
Molecular
viruses
chemical protein synthesis
Chemistry Techniques
Synthetic
Protein Synthesis
Dengue virus
medicine.disease_cause
010402 general chemistry
KAHA ligation
Chemical synthesis
01 natural sciences
Zuschrift
Catalysis
03 medical and health sciences
IFITM3
membrane proteins
protein modifications
medicine
Humans
Amino Acid Sequence
Proteinmodifikationen
Phosphorylation
Mode of action
Peptide sequence
Membranproteine
Fluorescent Dyes
Proteinsynthese
Ebola virus
Chemistry
Vesicle
Communication
Membrane Proteins
RNA-Binding Proteins
Zuschriften
General Chemistry
General Medicine
Transmembrane protein
Communications
3. Good health
0104 chemical sciences
030104 developmental biology
KAHA-Ligation
Biochemistry
Membrane protein
Chemische Proteinsynthese
Hydrophobic and Hydrophilic Interactions
Zdroj: Angewandte Chemie (International Ed. in English)
Angewandte Chemie International Edition
Angewandte Chemie. International Edition, 56 (41)
Angewandte Chemie (Weinheim an Der Bergstrasse, Germany)
ISSN: 1521-3773
1433-7851
Popis: Interferon-induced transmembrane protein 3 (IFITM3) is an antiviral transmembrane protein that is thought to serve as the primary factor for inhibiting the replication of a large number of viruses, including West Nile virus, Dengue virus, Ebola virus, and Zika virus. Production of this 14.5 kDa, 133-residue transmembrane protein, especially with essential posttranslational modifications, by recombinant expression is challenging. In this report, we document the chemical synthesis of IFTIM3 in multi-milligram quantities (>15 mg) and the preparation of phosphorylated and fluorescent variants. The synthesis was accomplished by using KAHA ligations, which operate under acidic aqueous/organic mixtures that excel at solubilizing even the exceptionally hydrophobic C-terminal region of IFITM3. The synthetic material is readily incorporated into model vesicles and forms the basis for using synthetic, homogenous IFITM3 and its derivatives for further studying its structure and biological mode of action. ISSN:1433-7851 ISSN:1521-3773 ISSN:0570-0833
Databáze: OpenAIRE
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