Effects of processing on structural, mechanical and biological properties of collagen-based substrates for regenerative medicine

A Terzi, E Storelli, Simona Bettini, T Sibillano, D. Altamura, Luca Salvatore, M Madaghiele, A Romano, D Siliqi, M Ladisa, L. De Caro, A Quattrini, Ludovico Valli, A Sannino, C Giannini

Research output: Contribution to journalArticle

Abstract

The aim of this work was to investigate the structural features of type I collagen isoforms and collagen-based films at atomic and molecular scales, in order to evaluate whether and to what extent different protocols of slurry synthesis may change the protein structure and the final properties of the developed scaffolds. Wide Angle X-ray Scattering data on raw materials demonstrated the preferential orientation of collagen molecules in equine tendon-derived collagens, while randomly oriented molecules were found in bovine skin collagens, together with a lower crystalline degree, analyzed by the assessment of FWHM (Full Width at Half Maximum), and a certain degree of salt contamination. WAXS and FT-IR (Fourier Transform Infrared) analyses on bovine collagen-based films, showed that mechanical homogenization of slurry in acidic solution was the treatment ensuring a high content of super-organization of collagen into triple helices and a high crystalline domain into the material. In vitro tests on rat Schwannoma cells showed that Schwann cell differentiation into myelinating cells was dependent on the specific collagen film being used, and was found to be stimulated in case of homogenization-treated samples. Finally DHT/EDC crosslinking treatment was shown to affect mechanical stiffness of films depending on collagen source and processing conditions. © 2018 The Author(s).
Original languageEnglish
Article number1429
JournalScientific Reports
Volume8
Issue number1
DOIs
Publication statusPublished - 2018

Fingerprint

Regenerative Medicine
Collagen
Schwann Cells
Neurilemmoma
Fourier Analysis
Collagen Type I
Tendons
Horses
Cell Differentiation
Protein Isoforms
Salts
X-Rays
Skin

Cite this

Effects of processing on structural, mechanical and biological properties of collagen-based substrates for regenerative medicine. / Terzi, A; Storelli, E; Bettini, Simona; Sibillano, T; Altamura, D.; Salvatore, Luca; Madaghiele, M; Romano, A; Siliqi, D; Ladisa, M; De Caro, L.; Quattrini, A; Valli, Ludovico; Sannino, A; Giannini, C.

In: Scientific Reports, Vol. 8, No. 1, 1429, 2018.

Research output: Contribution to journalArticle

Terzi, A, Storelli, E, Bettini, S, Sibillano, T, Altamura, D, Salvatore, L, Madaghiele, M, Romano, A, Siliqi, D, Ladisa, M, De Caro, L, Quattrini, A, Valli, L, Sannino, A & Giannini, C 2018, 'Effects of processing on structural, mechanical and biological properties of collagen-based substrates for regenerative medicine', Scientific Reports, vol. 8, no. 1, 1429. https://doi.org/10.1038/s41598-018-19786-0
Terzi, A ; Storelli, E ; Bettini, Simona ; Sibillano, T ; Altamura, D. ; Salvatore, Luca ; Madaghiele, M ; Romano, A ; Siliqi, D ; Ladisa, M ; De Caro, L. ; Quattrini, A ; Valli, Ludovico ; Sannino, A ; Giannini, C. / Effects of processing on structural, mechanical and biological properties of collagen-based substrates for regenerative medicine. In: Scientific Reports. 2018 ; Vol. 8, No. 1.
@article{b62e7b2eb4234fd8881b68fe4e077983,
title = "Effects of processing on structural, mechanical and biological properties of collagen-based substrates for regenerative medicine",
abstract = "The aim of this work was to investigate the structural features of type I collagen isoforms and collagen-based films at atomic and molecular scales, in order to evaluate whether and to what extent different protocols of slurry synthesis may change the protein structure and the final properties of the developed scaffolds. Wide Angle X-ray Scattering data on raw materials demonstrated the preferential orientation of collagen molecules in equine tendon-derived collagens, while randomly oriented molecules were found in bovine skin collagens, together with a lower crystalline degree, analyzed by the assessment of FWHM (Full Width at Half Maximum), and a certain degree of salt contamination. WAXS and FT-IR (Fourier Transform Infrared) analyses on bovine collagen-based films, showed that mechanical homogenization of slurry in acidic solution was the treatment ensuring a high content of super-organization of collagen into triple helices and a high crystalline domain into the material. In vitro tests on rat Schwannoma cells showed that Schwann cell differentiation into myelinating cells was dependent on the specific collagen film being used, and was found to be stimulated in case of homogenization-treated samples. Finally DHT/EDC crosslinking treatment was shown to affect mechanical stiffness of films depending on collagen source and processing conditions. {\circledC} 2018 The Author(s).",
author = "A Terzi and E Storelli and Simona Bettini and T Sibillano and D. Altamura and Luca Salvatore and M Madaghiele and A Romano and D Siliqi and M Ladisa and {De Caro}, L. and A Quattrini and Ludovico Valli and A Sannino and C Giannini",
year = "2018",
doi = "10.1038/s41598-018-19786-0",
language = "English",
volume = "8",
journal = "Scientific Reports",
issn = "2045-2322",
publisher = "Nature Publishing Group",
number = "1",

}

TY - JOUR

T1 - Effects of processing on structural, mechanical and biological properties of collagen-based substrates for regenerative medicine

AU - Terzi, A

AU - Storelli, E

AU - Bettini, Simona

AU - Sibillano, T

AU - Altamura, D.

AU - Salvatore, Luca

AU - Madaghiele, M

AU - Romano, A

AU - Siliqi, D

AU - Ladisa, M

AU - De Caro, L.

AU - Quattrini, A

AU - Valli, Ludovico

AU - Sannino, A

AU - Giannini, C

PY - 2018

Y1 - 2018

N2 - The aim of this work was to investigate the structural features of type I collagen isoforms and collagen-based films at atomic and molecular scales, in order to evaluate whether and to what extent different protocols of slurry synthesis may change the protein structure and the final properties of the developed scaffolds. Wide Angle X-ray Scattering data on raw materials demonstrated the preferential orientation of collagen molecules in equine tendon-derived collagens, while randomly oriented molecules were found in bovine skin collagens, together with a lower crystalline degree, analyzed by the assessment of FWHM (Full Width at Half Maximum), and a certain degree of salt contamination. WAXS and FT-IR (Fourier Transform Infrared) analyses on bovine collagen-based films, showed that mechanical homogenization of slurry in acidic solution was the treatment ensuring a high content of super-organization of collagen into triple helices and a high crystalline domain into the material. In vitro tests on rat Schwannoma cells showed that Schwann cell differentiation into myelinating cells was dependent on the specific collagen film being used, and was found to be stimulated in case of homogenization-treated samples. Finally DHT/EDC crosslinking treatment was shown to affect mechanical stiffness of films depending on collagen source and processing conditions. © 2018 The Author(s).

AB - The aim of this work was to investigate the structural features of type I collagen isoforms and collagen-based films at atomic and molecular scales, in order to evaluate whether and to what extent different protocols of slurry synthesis may change the protein structure and the final properties of the developed scaffolds. Wide Angle X-ray Scattering data on raw materials demonstrated the preferential orientation of collagen molecules in equine tendon-derived collagens, while randomly oriented molecules were found in bovine skin collagens, together with a lower crystalline degree, analyzed by the assessment of FWHM (Full Width at Half Maximum), and a certain degree of salt contamination. WAXS and FT-IR (Fourier Transform Infrared) analyses on bovine collagen-based films, showed that mechanical homogenization of slurry in acidic solution was the treatment ensuring a high content of super-organization of collagen into triple helices and a high crystalline domain into the material. In vitro tests on rat Schwannoma cells showed that Schwann cell differentiation into myelinating cells was dependent on the specific collagen film being used, and was found to be stimulated in case of homogenization-treated samples. Finally DHT/EDC crosslinking treatment was shown to affect mechanical stiffness of films depending on collagen source and processing conditions. © 2018 The Author(s).

U2 - 10.1038/s41598-018-19786-0

DO - 10.1038/s41598-018-19786-0

M3 - Article

VL - 8

JO - Scientific Reports

JF - Scientific Reports

SN - 2045-2322

IS - 1

M1 - 1429

ER -