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Protein functionalization revised: N‐tert‐butoxycarbonylation as an elegant tool to circumvent protein crosslinking

Ine Van Nieuwenhove (UGent) , Birgit Stubbe (UGent) , Geert-Jan Graulus (UGent) , Sandra Van Vlierberghe (UGent) and Peter Dubruel (UGent)
(2014) MACROMOLECULAR RAPID COMMUNICATIONS. 35(15). p.1351-1355
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Abstract
The protection of primary amines available in proteins holds great potential to introduce a plethora of diverse functionalities along the protein backbone (e.g., via its carboxylic acid or alcohol moieties) while circumventing the crosslinking issue using conventional approaches. This paper reports on a straightforward and efficient proof-of-concept including the chemoselective N-tert-butyloxycarbonylation of the primary amines in the protein gelatin (gel-NH-BOC), followed by introducing crosslinkable methacrylamide moieties. The reaction is performed successfully under relatively mild conditions (50 °C). Following selective protein functionalization, the deprotection is realized by adding a catalytic amount of an aqueous hydrogen chloride solution. The present communication illustrates the occurrence of a straightforward and selective deprotection procedure, which is typically required to circumvent the occurrence of acidic hydrolysis of the protein backbone. The results hold promise for a large range of biomedical applications in which the presence of primary amines is essential for preserving the biological activity.
Keywords
carbodiimide coupling, gelatin, N-Boc protection, modification, HYDROGELS, GELATIN

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Chicago
Van Nieuwenhove, Ine, Birgit Stubbe, Geert-Jan Graulus, Sandra Van Vlierberghe, and Peter Dubruel. 2014. “Protein Functionalization Revised: N‐tert‐butoxycarbonylation as an Elegant Tool to Circumvent Protein Crosslinking.” Macromolecular Rapid Communications 35 (15): 1351–1355.
APA
Van Nieuwenhove, I., Stubbe, B., Graulus, G.-J., Van Vlierberghe, S., & Dubruel, P. (2014). Protein functionalization revised: N‐tert‐butoxycarbonylation as an elegant tool to circumvent protein crosslinking. MACROMOLECULAR RAPID COMMUNICATIONS, 35(15), 1351–1355.
Vancouver
1.
Van Nieuwenhove I, Stubbe B, Graulus G-J, Van Vlierberghe S, Dubruel P. Protein functionalization revised: N‐tert‐butoxycarbonylation as an elegant tool to circumvent protein crosslinking. MACROMOLECULAR RAPID COMMUNICATIONS. 2014;35(15):1351–5.
MLA
Van Nieuwenhove, Ine, Birgit Stubbe, Geert-Jan Graulus, et al. “Protein Functionalization Revised: N‐tert‐butoxycarbonylation as an Elegant Tool to Circumvent Protein Crosslinking.” MACROMOLECULAR RAPID COMMUNICATIONS 35.15 (2014): 1351–1355. Print.
@article{5661366,
  abstract     = {The protection of primary amines available in proteins holds great potential to introduce a plethora of diverse functionalities along the protein backbone (e.g., via its carboxylic acid or alcohol moieties) while circumventing the crosslinking issue using conventional approaches. This paper reports on a straightforward and efficient proof-of-concept including the chemoselective N-tert-butyloxycarbonylation of the primary amines in the protein gelatin (gel-NH-BOC), followed by introducing crosslinkable methacrylamide moieties. The reaction is performed successfully under relatively mild conditions (50 {\textdegree}C). Following selective protein functionalization, the deprotection is realized by adding a catalytic amount of an aqueous hydrogen chloride solution. The present communication illustrates the occurrence of a straightforward and selective deprotection procedure, which is typically required to circumvent the occurrence of acidic hydrolysis of the protein backbone. The results hold promise for a large range of biomedical applications in which the presence of primary amines is essential for preserving the biological activity.},
  author       = {Van Nieuwenhove, Ine and Stubbe, Birgit and Graulus, Geert-Jan and Van Vlierberghe, Sandra and Dubruel, Peter},
  issn         = {1022-1336},
  journal      = {MACROMOLECULAR RAPID COMMUNICATIONS},
  language     = {eng},
  number       = {15},
  pages        = {1351--1355},
  title        = {Protein functionalization revised: N\unmatched{2010}tert\unmatched{2010}butoxycarbonylation as an elegant tool to circumvent protein crosslinking},
  url          = {http://dx.doi.org/10.1002/marc.201400103},
  volume       = {35},
  year         = {2014},
}

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