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Engineering of Ribosome-inactivating Proteins for Improving Pharmacological Properties.
- Source :
-
Toxins [Toxins (Basel)] 2020 Mar 09; Vol. 12 (3). Date of Electronic Publication: 2020 Mar 09. - Publication Year :
- 2020
-
Abstract
- Ribosome-inactivating proteins (RIPs) are N-glycosidases, which depurinate a specific adenine residue in the conserved α-sarcin/ricin loop (α-SRL) of rRNA. This loop is important for anchoring elongation factor (EF-G for prokaryote or eEF2 for eukaryote) in mRNA translocation. Translation is inhibited after the attack. RIPs therefore may have been applied for anti-cancer, and anti-virus and other therapeutic applications. The main obstacles of treatment with RIPs include short plasma half-life, non-selective cytotoxicity and antigenicity. This review focuses on the strategies used to improve the pharmacological properties of RIPs on human immunodeficiency virus (HIV) and cancers. Coupling with polyethylene glycol (PEG) increases plasma time and reduces antigenicity. RIPs conjugated with antibodies to form immunotoxins increase the selective toxicity to target cells. The prospects for future development on the engineering of RIPs for improving their pharmacological properties are also discussed.
- Subjects :
- Animals
Anti-HIV Agents chemistry
Anti-HIV Agents pharmacology
Anti-HIV Agents therapeutic use
Antineoplastic Agents chemistry
Antineoplastic Agents pharmacology
Antineoplastic Agents therapeutic use
Dextrans chemistry
Dextrans pharmacology
Dextrans therapeutic use
Humans
Polyethylene Glycols chemistry
Polyethylene Glycols pharmacology
Polyethylene Glycols therapeutic use
Protein Engineering
Ribosome Inactivating Proteins chemistry
Ribosome Inactivating Proteins pharmacology
Ribosome Inactivating Proteins therapeutic use
Subjects
Details
- Language :
- English
- ISSN :
- 2072-6651
- Volume :
- 12
- Issue :
- 3
- Database :
- MEDLINE
- Journal :
- Toxins
- Publication Type :
- Academic Journal
- Accession number :
- 32182799
- Full Text :
- https://doi.org/10.3390/toxins12030167