About: Chemical Synthesis of the Highly Hydrophobic Antiviral Membrane‐Associated Protein IFITM3 and Modified Variants

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About: Chemical Synthesis of the Highly Hydrophobic Antiviral Membrane‐Associated Protein IFITM3 and Modified Variants Goto Sponge NotDistinct Permalink

An Entity of Type : schema:ScholarlyArticle, within Data Space : covidontheweb.inria.fr associated with source document(s)

Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	Chemical Synthesis of the Highly Hydrophobic Antiviral Membrane‐Associated Protein IFITM3 and Modified Variants
Creator	Bode, Jeffrey Harmand, Thibault Pattabiraman, Vijaya
Source	PMC
abstract	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.
has issue date	2017-09-07(xsd:dateTime)
bibo:doi	10.1002/anie.201707554
bibo:pmid	28834009
has license	cc-by-nc-nd
sha1sum (hex)	aa029dc2c3ba585c0f6a05b6a1cf54e5aa66073b
schema:url	https://doi.org/10.1002/anie.201707554
resource representing a document's title	Chemical Synthesis of the Highly Hydrophobic Antiviral Membrane‐Associated Protein IFITM3 and Modified Variants
has PubMed Central identifier	PMC5658968
has PubMed identifier	28834009
schema:publication	Angew Chem Int Ed Engl
resource representing a document's body	covid:aa029dc2c3ba585c0f6a05b6a1cf54e5aa66073b#body_text
is schema:about of	named entity 'HYDROPHOBIC' named entity 'ASSOCIATED' named entity 'MODIFIED' named entity 'ANTIVIRAL' named entity 'CHEMICAL SYNTHESIS' named entity 'HIGHLY' named entity 'VARIANTS' named entity 'IFITM3' named entity 'SUPPORTING INFORMATION' named entity 'PROTEIN ' named entity 'MEMBRANE' named entity 'Hydrophobic' named entity 'IFITM3' named entity 'Antiviral' named entity 'Chemical Synthesis' named entity 'Synthesis' named entity 'Hydrophobic' named entity 'Information' named entity 'Protein' named entity 'Chemical' named entity 'Antiviral' named entity 'Membrane' named entity 'Variants'
is part of of	Chemical Synthesis of the Highly Hydrophobic Antiviral Membrane‐Associated Protein IFITM3 and Modified Variants covid:aa029dc2c3ba585c0f6a05b6a1cf54e5aa66073b#body_text 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.

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