Grafting-from lipase: Utilization of a common amino acid residue as a new grafting site

Marina Kovaliov, Cooper Cheng, Boyle Cheng, Saadyah Averick

Research output: Contribution to journalArticlepeer-review

16 Scopus citations


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.

Original languageEnglish
Pages (from-to)4651-4659
Number of pages9
JournalPolymer Chemistry
Issue number37
StatePublished - 7 Oct 2018
Externally publishedYes

Bibliographical note

Publisher Copyright:
© 2018 The Royal Society of Chemistry.


We gratefully acknowledge The Army Research Office (Award# 68271-CH) Young Investigator Program (W911NF-17-1-0015) and the Neuroscience Institute at AHN for funding NMR measurements and instrumentation at Carnegie Mellon University which was partially supported by NSF (CHE-0130903 and CHE-1039870). The MALDI-TOF data were collected using instrumentation purchased with NSF grant award CHE-0839233.

FundersFunder number
Neuroscience Institute
National Science FoundationCHE-1039870, CHE-0130903
Army Research OfficeW911NF-17-1-0015, 68271-CH
Carnegie Mellon University


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