Grafting-from lipase: utilization of a common amino acid residue as a new grafting site. Issue 37 (24th August 2018)
- Record Type:
- Journal Article
- Title:
- Grafting-from lipase: utilization of a common amino acid residue as a new grafting site. Issue 37 (24th August 2018)
- Main Title:
- Grafting-from lipase: utilization of a common amino acid residue as a new grafting site
- Authors:
- Kovaliov, Marina
Cheng, Cooper
Cheng, Boyle
Averick, Saadyah - Abstract:
- Abstract : A previously overlooked amino acid residue was utilized to grow polymers from proteins. Abstract : Protein–polymer hybrids are used in a variety of fields including catalysis, detection, and therapeutics. The grafting-from method for the synthesis of these biohybrids has gained popularity due to the ease of synthesis and purification. In this method, an initiator or chain transfer agent (CTA) is ligated onto an amino acid residue, typically lysine or cysteine, and polymers are subsequently grown in situ . In this manuscript, we report the preparation of protein polymer hybrids by grafting-from a previously overlooked acidic amino acid residue (glutamic and aspartic acid) and compare our results to protein polymer hybrids, grafted from the traditional lysine residue. Herein, we conjugated an atom transfer radical polymerization (ATRP) initiator to acidic amino acid residues and lysine residues and grew polymers from Thermomyces lanuginosa lipase (TL). N -[3-( N, N -Dimethylamino)propyl] acrylamide was grafted from the TL initiator, and the enzymatic activity of protein polymer hybrids was compared. We found that the acidic residues are easily modified with multiple ATRP initiators and polymers are readily grown. Additionally, the hybrids grafted from acidic residues demonstrated a 50% increase in enzyme activity compared to those grafted from lysine residues. Moreover, the activity was higher than that of native lipase TL in both cases. The polymers that wereAbstract : A previously overlooked amino acid residue was utilized to grow polymers from proteins. Abstract : Protein–polymer hybrids are used in a variety of fields including catalysis, detection, and therapeutics. The grafting-from method for the synthesis of these biohybrids has gained popularity due to the ease of synthesis and purification. In this method, an initiator or chain transfer agent (CTA) is ligated onto an amino acid residue, typically lysine or cysteine, and polymers are subsequently grown in situ . In this manuscript, we report the preparation of protein polymer hybrids by grafting-from a previously overlooked acidic amino acid residue (glutamic and aspartic acid) and compare our results to protein polymer hybrids, grafted from the traditional lysine residue. Herein, we conjugated an atom transfer radical polymerization (ATRP) initiator to acidic amino acid residues and lysine residues and grew polymers from Thermomyces lanuginosa lipase (TL). N -[3-( N, N -Dimethylamino)propyl] acrylamide was grafted from the TL initiator, and the enzymatic activity of protein polymer hybrids was compared. We found that the acidic residues are easily modified with multiple ATRP initiators and polymers are readily grown. Additionally, the hybrids grafted from acidic residues demonstrated a 50% increase in enzyme activity compared to those grafted from lysine residues. Moreover, the activity was higher than that of native lipase TL in both cases. The polymers that were grafted-from the acid residues tended to provide the hybrids with a higher activity at elevated temperatures. These results point to a new amino acid ligation strategy for preparing protein polymer hybrids via a grafting-from method. … (more)
- Is Part Of:
- Polymer chemistry. Volume 9:Issue 37(2018)
- Journal:
- Polymer chemistry
- Issue:
- Volume 9:Issue 37(2018)
- Issue Display:
- Volume 9, Issue 37 (2018)
- Year:
- 2018
- Volume:
- 9
- Issue:
- 37
- Issue Sort Value:
- 2018-0009-0037-0000
- Page Start:
- 4651
- Page End:
- 4659
- Publication Date:
- 2018-08-24
- Subjects:
- Polymers -- Periodicals
Macromolecules -- Periodicals
Polymerization -- Periodicals
547.705 - Journal URLs:
- http://www.rsc.org/Publishing/Journals/PY/Index.asp ↗
http://www.rsc.org/ ↗ - DOI:
- 10.1039/c8py01026a ↗
- Languages:
- English
- ISSNs:
- 1759-9954
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 6547.703400
British Library DSC - BLDSS-3PM
British Library STI - ELD Digital store - Ingest File:
- 7674.xml