Structural Breakdown of Collagen Type I Elastin Blend Polymerization
Biopolymer blends are advantageous materials with novel properties that may show performances way beyond their individual constituents. Collagen elastin hybrid gels are a new representative of such materials as they employ elastin’s thermo switching behavior in the physiological temperature regime....
| Main Authors: | , , , |
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| Format: | Article |
| Language: | English |
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MDPI AG
2022-10-01
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| Series: | Polymers |
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| Online Access: | https://www.mdpi.com/2073-4360/14/20/4434 |
| _version_ | 1797470146882699264 |
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| author | Nils Wilharm Tony Fischer Alexander Hayn Stefan G. Mayr |
| author_facet | Nils Wilharm Tony Fischer Alexander Hayn Stefan G. Mayr |
| author_sort | Nils Wilharm |
| collection | DOAJ |
| description | Biopolymer blends are advantageous materials with novel properties that may show performances way beyond their individual constituents. Collagen elastin hybrid gels are a new representative of such materials as they employ elastin’s thermo switching behavior in the physiological temperature regime. Although recent studies highlight the potential applications of such systems, little is known about the interaction of collagen and elastin fibers during polymerization. In fact, the final network structure is predetermined in the early and mostly arbitrary association of the fibers. We investigated type I collagen polymerized with bovine neck ligament elastin with up to 33.3 weight percent elastin and showed, by using a plate reader, zeta potential and laser scanning microscopy (LSM) experiments, that elastin fibers bind in a lateral manner to collagen fibers. Our plate reader experiments revealed an elastin concentration-dependent increase in the polymerization rate, although the rate increase was greatest at intermediate elastin concentrations. As elastin does not significantly change the structural metrics pore size, fiber thickness or 2D anisotropy of the final gel, we are confident to conclude that elastin is incorporated homogeneously into the collagen fibers. |
| first_indexed | 2024-03-09T19:32:37Z |
| format | Article |
| id | doaj.art-6090dbe57c05419c8cc18920313c258c |
| institution | Directory Open Access Journal |
| issn | 2073-4360 |
| language | English |
| last_indexed | 2024-03-09T19:32:37Z |
| publishDate | 2022-10-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Polymers |
| spelling | doaj.art-6090dbe57c05419c8cc18920313c258c2023-11-24T02:09:23ZengMDPI AGPolymers2073-43602022-10-011420443410.3390/polym14204434Structural Breakdown of Collagen Type I Elastin Blend PolymerizationNils Wilharm0Tony Fischer1Alexander Hayn2Stefan G. Mayr3Leibniz-Institut für Oberflächenmodifizierung e.V. (IOM), Permoserstr. 15, 04318 Leipzig, GermanyBiological Physics Division, Department of Physics and Earth Sciences, Leipzig University, Linnéstraße 5, 04103 Leipzig, GermanyBiological Physics Division, Department of Physics and Earth Sciences, Leipzig University, Linnéstraße 5, 04103 Leipzig, GermanyLeibniz-Institut für Oberflächenmodifizierung e.V. (IOM), Permoserstr. 15, 04318 Leipzig, GermanyBiopolymer blends are advantageous materials with novel properties that may show performances way beyond their individual constituents. Collagen elastin hybrid gels are a new representative of such materials as they employ elastin’s thermo switching behavior in the physiological temperature regime. Although recent studies highlight the potential applications of such systems, little is known about the interaction of collagen and elastin fibers during polymerization. In fact, the final network structure is predetermined in the early and mostly arbitrary association of the fibers. We investigated type I collagen polymerized with bovine neck ligament elastin with up to 33.3 weight percent elastin and showed, by using a plate reader, zeta potential and laser scanning microscopy (LSM) experiments, that elastin fibers bind in a lateral manner to collagen fibers. Our plate reader experiments revealed an elastin concentration-dependent increase in the polymerization rate, although the rate increase was greatest at intermediate elastin concentrations. As elastin does not significantly change the structural metrics pore size, fiber thickness or 2D anisotropy of the final gel, we are confident to conclude that elastin is incorporated homogeneously into the collagen fibers.https://www.mdpi.com/2073-4360/14/20/4434elastincollagenpolymerizationfiber formation |
| spellingShingle | Nils Wilharm Tony Fischer Alexander Hayn Stefan G. Mayr Structural Breakdown of Collagen Type I Elastin Blend Polymerization Polymers elastin collagen polymerization fiber formation |
| title | Structural Breakdown of Collagen Type I Elastin Blend Polymerization |
| title_full | Structural Breakdown of Collagen Type I Elastin Blend Polymerization |
| title_fullStr | Structural Breakdown of Collagen Type I Elastin Blend Polymerization |
| title_full_unstemmed | Structural Breakdown of Collagen Type I Elastin Blend Polymerization |
| title_short | Structural Breakdown of Collagen Type I Elastin Blend Polymerization |
| title_sort | structural breakdown of collagen type i elastin blend polymerization |
| topic | elastin collagen polymerization fiber formation |
| url | https://www.mdpi.com/2073-4360/14/20/4434 |
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