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Assessing Collagen D-Band Periodicity with Atomic Force Microscopy

The collagen superfamily includes more than fifty collagen and/or collagen-like proteins with fibril-forming collagen type I being the most abundant protein within the extracellular matrix. Collagen type I plays a crucial role in a variety of functions, it has been associated with many pathological...

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Autor principal: Stylianou, Andreas
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8877100/
https://www.ncbi.nlm.nih.gov/pubmed/35208148
http://dx.doi.org/10.3390/ma15041608
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author Stylianou, Andreas
author_facet Stylianou, Andreas
author_sort Stylianou, Andreas
collection PubMed
description The collagen superfamily includes more than fifty collagen and/or collagen-like proteins with fibril-forming collagen type I being the most abundant protein within the extracellular matrix. Collagen type I plays a crucial role in a variety of functions, it has been associated with many pathological conditions and it is widely used due to its unique properties. One unique nano-scale characteristic of natural occurring collagen type I fibers is the so-called D-band periodicity, which has been associated with collagen natural structure and properties, while it seems to play a crucial role in the interactions between cells and collagen and in various pathological conditions. An accurate characterization of the surface and structure of collagen fibers, including D-band periodicity, on collagen-based tissues and/or (nano-)biomaterials can be achieved by Atomic Force Microscopy (AFM). AFM is a scanning probe microscope and is among the few techniques that can assess D-band periodicity. This review covers issues related to collagen and collagen D-band periodicity and the use of AFM for studying them. Through a systematic search in databases (PubMed and Scopus) relevant articles were identified. The study of these articles demonstrated that AFM can offer novel information concerning D-band periodicity. This study highlights the importance of studying collagen D-band periodicity and proves that AFM is a powerful tool for investigating a number of different properties related to collagen D-band periodicity.
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spelling pubmed-88771002022-02-26 Assessing Collagen D-Band Periodicity with Atomic Force Microscopy Stylianou, Andreas Materials (Basel) Review The collagen superfamily includes more than fifty collagen and/or collagen-like proteins with fibril-forming collagen type I being the most abundant protein within the extracellular matrix. Collagen type I plays a crucial role in a variety of functions, it has been associated with many pathological conditions and it is widely used due to its unique properties. One unique nano-scale characteristic of natural occurring collagen type I fibers is the so-called D-band periodicity, which has been associated with collagen natural structure and properties, while it seems to play a crucial role in the interactions between cells and collagen and in various pathological conditions. An accurate characterization of the surface and structure of collagen fibers, including D-band periodicity, on collagen-based tissues and/or (nano-)biomaterials can be achieved by Atomic Force Microscopy (AFM). AFM is a scanning probe microscope and is among the few techniques that can assess D-band periodicity. This review covers issues related to collagen and collagen D-band periodicity and the use of AFM for studying them. Through a systematic search in databases (PubMed and Scopus) relevant articles were identified. The study of these articles demonstrated that AFM can offer novel information concerning D-band periodicity. This study highlights the importance of studying collagen D-band periodicity and proves that AFM is a powerful tool for investigating a number of different properties related to collagen D-band periodicity. MDPI 2022-02-21 /pmc/articles/PMC8877100/ /pubmed/35208148 http://dx.doi.org/10.3390/ma15041608 Text en © 2022 by the author. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).
spellingShingle Review
Stylianou, Andreas
Assessing Collagen D-Band Periodicity with Atomic Force Microscopy
title Assessing Collagen D-Band Periodicity with Atomic Force Microscopy
title_full Assessing Collagen D-Band Periodicity with Atomic Force Microscopy
title_fullStr Assessing Collagen D-Band Periodicity with Atomic Force Microscopy
title_full_unstemmed Assessing Collagen D-Band Periodicity with Atomic Force Microscopy
title_short Assessing Collagen D-Band Periodicity with Atomic Force Microscopy
title_sort assessing collagen d-band periodicity with atomic force microscopy
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8877100/
https://www.ncbi.nlm.nih.gov/pubmed/35208148
http://dx.doi.org/10.3390/ma15041608
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