Grafting-from lipase: utilization of a common amino acid residue as a new grafting site
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...
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Published in | Polymer chemistry Vol. 9; no. 37; pp. 4651 - 4659 |
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Main Authors | , , , |
Format | Journal Article |
Language | English |
Published |
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Royal Society of Chemistry
07.10.2018
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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. |
---|---|
AbstractList | 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. 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. |
Author | Cheng, Cooper Kovaliov, Marina Cheng, Boyle Averick, Saadyah |
Author_xml | – sequence: 1 givenname: Marina surname: Kovaliov fullname: Kovaliov, Marina organization: Neuroscience Disruptive Research Lab, Allegheny Health Network Research Institute, Allegheny General Hospital, Pitts-burgh, USA – sequence: 2 givenname: Cooper surname: Cheng fullname: Cheng, Cooper organization: Neuroscience Disruptive Research Lab, Allegheny Health Network Research Institute, Allegheny General Hospital, Pitts-burgh, USA – sequence: 3 givenname: Boyle surname: Cheng fullname: Cheng, Boyle organization: Neuroscience Institute, Allegheny Health Network, Allegheny General Hospital, Pittsburgh, USA – sequence: 4 givenname: Saadyah orcidid: 0000-0003-4775-2317 surname: Averick fullname: Averick, Saadyah organization: Neuroscience Disruptive Research Lab, Allegheny Health Network Research Institute, Allegheny General Hospital, Pitts-burgh, USA |
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CitedBy_id | crossref_primary_10_1039_C8PY01399C crossref_primary_10_1039_C9PY01462D crossref_primary_10_1134_S1811238222700035 crossref_primary_10_1002_marc_202200195 crossref_primary_10_1016_j_polymer_2020_123062 crossref_primary_10_3389_fbioe_2020_00830 crossref_primary_10_1016_j_cjche_2023_04_005 crossref_primary_10_1021_acs_chemrev_0c01201 crossref_primary_10_1016_j_progpolymsci_2019_101186 crossref_primary_10_3390_polym15051234 crossref_primary_10_1016_j_bej_2023_108851 crossref_primary_10_1016_j_bej_2021_108025 crossref_primary_10_1007_s12649_022_01735_8 crossref_primary_10_1021_acs_langmuir_1c00755 crossref_primary_10_1021_acs_bioconjchem_0c00084 |
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SubjectTerms | Acrylamide Addition polymerization Amino acids Aspartic acid Catalysis Chain transfer Chemical synthesis Enzyme activity Grafting High temperature Initiators Lipase Lysine Polymer chemistry Polymers Proteins Residues |
Title | Grafting-from lipase: utilization of a common amino acid residue as a new grafting site |
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