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Effect of Silicone on the Collagen Fibrillogenesis and Stability

Collagen, the most abundant protein in mammals, is able to form fibrils, which have central role in tissue repair, fibrosis, and tumor invasion. As a component of skin, tendons, and cartilages, this protein contacts with any implanted materials. An inherent problem associated with implanted prosthes...

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Autores principales: Kadziński, Leszek, Prokopowicz, Magdalena, Jakóbkiewicz-Banecka, Joanna, Gabig-Cimińska, Magdalena, Łukasiak, Jerzy, Banecki, Bogdan
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Blackwell Publishing Ltd 2015
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4418381/
https://www.ncbi.nlm.nih.gov/pubmed/25589402
http://dx.doi.org/10.1002/jps.24351
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author Kadziński, Leszek
Prokopowicz, Magdalena
Jakóbkiewicz-Banecka, Joanna
Gabig-Cimińska, Magdalena
Łukasiak, Jerzy
Banecki, Bogdan
author_facet Kadziński, Leszek
Prokopowicz, Magdalena
Jakóbkiewicz-Banecka, Joanna
Gabig-Cimińska, Magdalena
Łukasiak, Jerzy
Banecki, Bogdan
author_sort Kadziński, Leszek
collection PubMed
description Collagen, the most abundant protein in mammals, is able to form fibrils, which have central role in tissue repair, fibrosis, and tumor invasion. As a component of skin, tendons, and cartilages, this protein contacts with any implanted materials. An inherent problem associated with implanted prostheses is their propensity to be coated with host proteins shortly after implantation. Also, silicone implants undergoing relatively long periods of contact with blood can lead to formation of thrombi and emboli. In this paper, we demonstrate the existence of interactions between siloxanes and collagen. Low-molecular-weight cyclic siloxane (hexamethylcyclotrisiloxane—D3) and polydimethylsiloxanes (PDMS) forming linear chains, ranging in viscosity from 20 to 12,000 cSt, were analyzed. We show that D3 as well as short-chain PDMS interact with collagen, resulting in a decrease in fibrillogenesis. However, loss of collagen native structure does not occur because of these interactions. Rather, collagen seems to be sequestered in its native form in an interlayer formed by collagen–siloxane complexes. On the other hand, silicone molecules with longer chains (i.e., PDMS with viscosity of 1000 and 12,000 cSt, the highest viscosity analyzed here) demonstrate little interaction with this protein and do not seem to affect collagen activity. © 2015 Wiley Periodicals, Inc. and the American Pharmacists Association J Pharm Sci 104:1275–1281, 2015
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spelling pubmed-44183812015-05-06 Effect of Silicone on the Collagen Fibrillogenesis and Stability Kadziński, Leszek Prokopowicz, Magdalena Jakóbkiewicz-Banecka, Joanna Gabig-Cimińska, Magdalena Łukasiak, Jerzy Banecki, Bogdan J Pharm Sci Pharmaceutical Biotechnology Collagen, the most abundant protein in mammals, is able to form fibrils, which have central role in tissue repair, fibrosis, and tumor invasion. As a component of skin, tendons, and cartilages, this protein contacts with any implanted materials. An inherent problem associated with implanted prostheses is their propensity to be coated with host proteins shortly after implantation. Also, silicone implants undergoing relatively long periods of contact with blood can lead to formation of thrombi and emboli. In this paper, we demonstrate the existence of interactions between siloxanes and collagen. Low-molecular-weight cyclic siloxane (hexamethylcyclotrisiloxane—D3) and polydimethylsiloxanes (PDMS) forming linear chains, ranging in viscosity from 20 to 12,000 cSt, were analyzed. We show that D3 as well as short-chain PDMS interact with collagen, resulting in a decrease in fibrillogenesis. However, loss of collagen native structure does not occur because of these interactions. Rather, collagen seems to be sequestered in its native form in an interlayer formed by collagen–siloxane complexes. On the other hand, silicone molecules with longer chains (i.e., PDMS with viscosity of 1000 and 12,000 cSt, the highest viscosity analyzed here) demonstrate little interaction with this protein and do not seem to affect collagen activity. © 2015 Wiley Periodicals, Inc. and the American Pharmacists Association J Pharm Sci 104:1275–1281, 2015 Blackwell Publishing Ltd 2015-04 2015-01-14 /pmc/articles/PMC4418381/ /pubmed/25589402 http://dx.doi.org/10.1002/jps.24351 Text en © 2015 The Authors. Journal of Pharmaceutical Sciences published by Wiley Periodicals, Inc. and the American Pharmacists Association http://creativecommons.org/licenses/by-nc/4.0/ This is an open access article under the terms of the Creative Commons Attribution-NonCommercial License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited and is not used for commercial purposes.
spellingShingle Pharmaceutical Biotechnology
Kadziński, Leszek
Prokopowicz, Magdalena
Jakóbkiewicz-Banecka, Joanna
Gabig-Cimińska, Magdalena
Łukasiak, Jerzy
Banecki, Bogdan
Effect of Silicone on the Collagen Fibrillogenesis and Stability
title Effect of Silicone on the Collagen Fibrillogenesis and Stability
title_full Effect of Silicone on the Collagen Fibrillogenesis and Stability
title_fullStr Effect of Silicone on the Collagen Fibrillogenesis and Stability
title_full_unstemmed Effect of Silicone on the Collagen Fibrillogenesis and Stability
title_short Effect of Silicone on the Collagen Fibrillogenesis and Stability
title_sort effect of silicone on the collagen fibrillogenesis and stability
topic Pharmaceutical Biotechnology
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4418381/
https://www.ncbi.nlm.nih.gov/pubmed/25589402
http://dx.doi.org/10.1002/jps.24351
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