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Ultra‐Rapid and Specific Gelation of Collagen Molecules for Transparent and Tough Gels by Transition Metal Complexation

Collagen is the most abundant protein in the human body and one of the main components of stromal tissues in tumors which have a high elastic modulus of over 50 kPa. Although collagen has been widely used as a cell culture scaffold for cancer cells, there have been limitations when attempting to fab...

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Autores principales: Suezawa, Tomoyuki, Sasaki, Naoko, Yukawa, Yuichi, Assan, Nazgul, Uetake, Yuta, Onuma, Kunishige, Kamada, Rino, Tomioka, Daisuke, Sakurai, Hidehiro, Katayama, Ryohei, Inoue, Masahiro, Matsusaki, Michiya
Formato: Online Artículo Texto
Lenguaje:English
Publicado: John Wiley and Sons Inc. 2023
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10602541/
https://www.ncbi.nlm.nih.gov/pubmed/37697642
http://dx.doi.org/10.1002/advs.202302637
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author Suezawa, Tomoyuki
Sasaki, Naoko
Yukawa, Yuichi
Assan, Nazgul
Uetake, Yuta
Onuma, Kunishige
Kamada, Rino
Tomioka, Daisuke
Sakurai, Hidehiro
Katayama, Ryohei
Inoue, Masahiro
Matsusaki, Michiya
author_facet Suezawa, Tomoyuki
Sasaki, Naoko
Yukawa, Yuichi
Assan, Nazgul
Uetake, Yuta
Onuma, Kunishige
Kamada, Rino
Tomioka, Daisuke
Sakurai, Hidehiro
Katayama, Ryohei
Inoue, Masahiro
Matsusaki, Michiya
author_sort Suezawa, Tomoyuki
collection PubMed
description Collagen is the most abundant protein in the human body and one of the main components of stromal tissues in tumors which have a high elastic modulus of over 50 kPa. Although collagen has been widely used as a cell culture scaffold for cancer cells, there have been limitations when attempting to fabricate a tough collagen gel with cells like a cancer stroma. Here, rapid gelation of a collagen solution within a few minutes by transition metal complexation is demonstrated. Type I collagen solution at neutral pH shows rapid gelation with a transparency of 81% and a high modulus of 1,781 kPa by mixing with K(2)PtCl(4) solution within 3 min. Other transition metal ions also show the same rapid gelation, but not basic metal ions. Interestingly, although type I to IV collagen molecules show rapid gelation, other extracellular matrices  do not exhibit this phenomenon. Live imaging of colon cancer organoids in 3D culture indicates a collective migration property with modulating high elastic modulus, suggesting activation for metastasis progress. This technology will be useful as a new class of 3D culture for cells and organoids due to its facility for deep‐live observation and mechanical stiffness adjustment.
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spelling pubmed-106025412023-10-27 Ultra‐Rapid and Specific Gelation of Collagen Molecules for Transparent and Tough Gels by Transition Metal Complexation Suezawa, Tomoyuki Sasaki, Naoko Yukawa, Yuichi Assan, Nazgul Uetake, Yuta Onuma, Kunishige Kamada, Rino Tomioka, Daisuke Sakurai, Hidehiro Katayama, Ryohei Inoue, Masahiro Matsusaki, Michiya Adv Sci (Weinh) Research Articles Collagen is the most abundant protein in the human body and one of the main components of stromal tissues in tumors which have a high elastic modulus of over 50 kPa. Although collagen has been widely used as a cell culture scaffold for cancer cells, there have been limitations when attempting to fabricate a tough collagen gel with cells like a cancer stroma. Here, rapid gelation of a collagen solution within a few minutes by transition metal complexation is demonstrated. Type I collagen solution at neutral pH shows rapid gelation with a transparency of 81% and a high modulus of 1,781 kPa by mixing with K(2)PtCl(4) solution within 3 min. Other transition metal ions also show the same rapid gelation, but not basic metal ions. Interestingly, although type I to IV collagen molecules show rapid gelation, other extracellular matrices  do not exhibit this phenomenon. Live imaging of colon cancer organoids in 3D culture indicates a collective migration property with modulating high elastic modulus, suggesting activation for metastasis progress. This technology will be useful as a new class of 3D culture for cells and organoids due to its facility for deep‐live observation and mechanical stiffness adjustment. John Wiley and Sons Inc. 2023-09-11 /pmc/articles/PMC10602541/ /pubmed/37697642 http://dx.doi.org/10.1002/advs.202302637 Text en © 2023 The Authors. Advanced Science published by Wiley‐VCH GmbH https://creativecommons.org/licenses/by/4.0/This is an open access article under the terms of the http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.
spellingShingle Research Articles
Suezawa, Tomoyuki
Sasaki, Naoko
Yukawa, Yuichi
Assan, Nazgul
Uetake, Yuta
Onuma, Kunishige
Kamada, Rino
Tomioka, Daisuke
Sakurai, Hidehiro
Katayama, Ryohei
Inoue, Masahiro
Matsusaki, Michiya
Ultra‐Rapid and Specific Gelation of Collagen Molecules for Transparent and Tough Gels by Transition Metal Complexation
title Ultra‐Rapid and Specific Gelation of Collagen Molecules for Transparent and Tough Gels by Transition Metal Complexation
title_full Ultra‐Rapid and Specific Gelation of Collagen Molecules for Transparent and Tough Gels by Transition Metal Complexation
title_fullStr Ultra‐Rapid and Specific Gelation of Collagen Molecules for Transparent and Tough Gels by Transition Metal Complexation
title_full_unstemmed Ultra‐Rapid and Specific Gelation of Collagen Molecules for Transparent and Tough Gels by Transition Metal Complexation
title_short Ultra‐Rapid and Specific Gelation of Collagen Molecules for Transparent and Tough Gels by Transition Metal Complexation
title_sort ultra‐rapid and specific gelation of collagen molecules for transparent and tough gels by transition metal complexation
topic Research Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10602541/
https://www.ncbi.nlm.nih.gov/pubmed/37697642
http://dx.doi.org/10.1002/advs.202302637
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