Development of a Human Recombinant Collagen for Vat Polymerization-Based Bioprinting

Research output: Contribution to journalArticleResearchpeer review

Authors

Research Organisations

External Research Organisations

  • Cellbricks GmbH
View graph of relations

Details

Original languageEnglish
Article numbere202400393
JournalBiotechnology journal
Volume19
Issue number10
Publication statusPublished - 9 Oct 2024

Abstract

In light-based 3D-bioprinting, gelatin methacrylate (GelMA) is one of the most widely used materials, as it supports cell attachment, and shows good biocompatibility and degradability in vivo. However, as an animal-derived material, it also causes safety concerns when used in medical applications. Gelatin is a partial hydrolysate of collagen, containing high amounts of hydroxyproline. This causes the material to form a thermally induced gel at ambient temperatures, a behavior also observed in GelMA. This temperature-dependent gelation requires precise temperature control during the bioprinting process to prevent the gelation of the material. To avoid safety concerns associated with animal-derived materials and reduce potential issues caused by thermal gelation, a recombinant human alpha-1 collagen I fragment was expressed in Komagataella phaffii without hydroxylation. The resulting protein was successfully modified with methacryloyl groups and underwent rapid photopolymerization upon ultraviolet light exposure. The developed material exhibited slightly slower polymerization and lower storage modulus compared to GelMA, while it showed higher stretchability. However, unlike the latter, the material did not undergo physical gelation at ambient temperatures, but only when cooled down to below 10°C, a characteristic that has not been described for comparable materials so far. This gelation was not caused by the formation of triple-helical structures, as shown by the absence of the characteristic peak at 220 nm in CD spectra. Moreover, the developed recombinant material facilitated cell adherence with high cell viability after crosslinking via light to a 3D structure. Furthermore, desired geometries could be easily printed on a stereolithographic bioprinter.

Keywords

    GelMA, recombinant bioink, recombinant gelatin, thermal gelling

ASJC Scopus subject areas

Cite this

Development of a Human Recombinant Collagen for Vat Polymerization-Based Bioprinting. / Schlauch, Domenic; Ebbecke, Jan Peter; Meyer, Johanna et al.
In: Biotechnology journal, Vol. 19, No. 10, e202400393, 09.10.2024.

Research output: Contribution to journalArticleResearchpeer review

Schlauch, D, Ebbecke, JP, Meyer, J, Fleischhammer, TM, Pirmahboub, H, Kloke, L, Kara, S, Lavrentieva, A & Pepelanova, I 2024, 'Development of a Human Recombinant Collagen for Vat Polymerization-Based Bioprinting', Biotechnology journal, vol. 19, no. 10, e202400393. https://doi.org/10.1002/biot.202400393
Schlauch, D., Ebbecke, J. P., Meyer, J., Fleischhammer, T. M., Pirmahboub, H., Kloke, L., Kara, S., Lavrentieva, A., & Pepelanova, I. (2024). Development of a Human Recombinant Collagen for Vat Polymerization-Based Bioprinting. Biotechnology journal, 19(10), Article e202400393. https://doi.org/10.1002/biot.202400393
Schlauch D, Ebbecke JP, Meyer J, Fleischhammer TM, Pirmahboub H, Kloke L et al. Development of a Human Recombinant Collagen for Vat Polymerization-Based Bioprinting. Biotechnology journal. 2024 Oct 9;19(10):e202400393. doi: 10.1002/biot.202400393
Download
@article{27b43d5419e44a66b68f529d10f1abdc,
title = "Development of a Human Recombinant Collagen for Vat Polymerization-Based Bioprinting",
abstract = "In light-based 3D-bioprinting, gelatin methacrylate (GelMA) is one of the most widely used materials, as it supports cell attachment, and shows good biocompatibility and degradability in vivo. However, as an animal-derived material, it also causes safety concerns when used in medical applications. Gelatin is a partial hydrolysate of collagen, containing high amounts of hydroxyproline. This causes the material to form a thermally induced gel at ambient temperatures, a behavior also observed in GelMA. This temperature-dependent gelation requires precise temperature control during the bioprinting process to prevent the gelation of the material. To avoid safety concerns associated with animal-derived materials and reduce potential issues caused by thermal gelation, a recombinant human alpha-1 collagen I fragment was expressed in Komagataella phaffii without hydroxylation. The resulting protein was successfully modified with methacryloyl groups and underwent rapid photopolymerization upon ultraviolet light exposure. The developed material exhibited slightly slower polymerization and lower storage modulus compared to GelMA, while it showed higher stretchability. However, unlike the latter, the material did not undergo physical gelation at ambient temperatures, but only when cooled down to below 10°C, a characteristic that has not been described for comparable materials so far. This gelation was not caused by the formation of triple-helical structures, as shown by the absence of the characteristic peak at 220 nm in CD spectra. Moreover, the developed recombinant material facilitated cell adherence with high cell viability after crosslinking via light to a 3D structure. Furthermore, desired geometries could be easily printed on a stereolithographic bioprinter.",
keywords = "GelMA, recombinant bioink, recombinant gelatin, thermal gelling",
author = "Domenic Schlauch and Ebbecke, {Jan Peter} and Johanna Meyer and Fleischhammer, {Tabea Marie} and Hamidreza Pirmahboub and Lutz Kloke and Selin Kara and Antonina Lavrentieva and Iliyana Pepelanova",
note = "Publisher Copyright: {\textcopyright} 2024 The Author(s). Biotechnology Journal published by Wiley-VCH GmbH.",
year = "2024",
month = oct,
day = "9",
doi = "10.1002/biot.202400393",
language = "English",
volume = "19",
journal = "Biotechnology journal",
issn = "1860-6768",
publisher = "Wiley-VCH Verlag",
number = "10",

}

Download

TY - JOUR

T1 - Development of a Human Recombinant Collagen for Vat Polymerization-Based Bioprinting

AU - Schlauch, Domenic

AU - Ebbecke, Jan Peter

AU - Meyer, Johanna

AU - Fleischhammer, Tabea Marie

AU - Pirmahboub, Hamidreza

AU - Kloke, Lutz

AU - Kara, Selin

AU - Lavrentieva, Antonina

AU - Pepelanova, Iliyana

N1 - Publisher Copyright: © 2024 The Author(s). Biotechnology Journal published by Wiley-VCH GmbH.

PY - 2024/10/9

Y1 - 2024/10/9

N2 - In light-based 3D-bioprinting, gelatin methacrylate (GelMA) is one of the most widely used materials, as it supports cell attachment, and shows good biocompatibility and degradability in vivo. However, as an animal-derived material, it also causes safety concerns when used in medical applications. Gelatin is a partial hydrolysate of collagen, containing high amounts of hydroxyproline. This causes the material to form a thermally induced gel at ambient temperatures, a behavior also observed in GelMA. This temperature-dependent gelation requires precise temperature control during the bioprinting process to prevent the gelation of the material. To avoid safety concerns associated with animal-derived materials and reduce potential issues caused by thermal gelation, a recombinant human alpha-1 collagen I fragment was expressed in Komagataella phaffii without hydroxylation. The resulting protein was successfully modified with methacryloyl groups and underwent rapid photopolymerization upon ultraviolet light exposure. The developed material exhibited slightly slower polymerization and lower storage modulus compared to GelMA, while it showed higher stretchability. However, unlike the latter, the material did not undergo physical gelation at ambient temperatures, but only when cooled down to below 10°C, a characteristic that has not been described for comparable materials so far. This gelation was not caused by the formation of triple-helical structures, as shown by the absence of the characteristic peak at 220 nm in CD spectra. Moreover, the developed recombinant material facilitated cell adherence with high cell viability after crosslinking via light to a 3D structure. Furthermore, desired geometries could be easily printed on a stereolithographic bioprinter.

AB - In light-based 3D-bioprinting, gelatin methacrylate (GelMA) is one of the most widely used materials, as it supports cell attachment, and shows good biocompatibility and degradability in vivo. However, as an animal-derived material, it also causes safety concerns when used in medical applications. Gelatin is a partial hydrolysate of collagen, containing high amounts of hydroxyproline. This causes the material to form a thermally induced gel at ambient temperatures, a behavior also observed in GelMA. This temperature-dependent gelation requires precise temperature control during the bioprinting process to prevent the gelation of the material. To avoid safety concerns associated with animal-derived materials and reduce potential issues caused by thermal gelation, a recombinant human alpha-1 collagen I fragment was expressed in Komagataella phaffii without hydroxylation. The resulting protein was successfully modified with methacryloyl groups and underwent rapid photopolymerization upon ultraviolet light exposure. The developed material exhibited slightly slower polymerization and lower storage modulus compared to GelMA, while it showed higher stretchability. However, unlike the latter, the material did not undergo physical gelation at ambient temperatures, but only when cooled down to below 10°C, a characteristic that has not been described for comparable materials so far. This gelation was not caused by the formation of triple-helical structures, as shown by the absence of the characteristic peak at 220 nm in CD spectra. Moreover, the developed recombinant material facilitated cell adherence with high cell viability after crosslinking via light to a 3D structure. Furthermore, desired geometries could be easily printed on a stereolithographic bioprinter.

KW - GelMA

KW - recombinant bioink

KW - recombinant gelatin

KW - thermal gelling

UR - http://www.scopus.com/inward/record.url?scp=85206023336&partnerID=8YFLogxK

U2 - 10.1002/biot.202400393

DO - 10.1002/biot.202400393

M3 - Article

C2 - 39380502

AN - SCOPUS:85206023336

VL - 19

JO - Biotechnology journal

JF - Biotechnology journal

SN - 1860-6768

IS - 10

M1 - e202400393

ER -