Loading…
Type-I collagen fibrils: From growth morphology to local order
. The length of type-I collagen fibrils in solution increases through the development and progress of pointed tips appearing successively at the two ends of an axis-symmetric shaft with constant diameter. Those tips, respectively fine ( α ) or coarse ( β ) have opposite molecular orientations. The α...
Saved in:
| Published in: | The European physical journal. E, Soft matter and biological physics Soft matter and biological physics, 2019-04, Vol.42 (4), p.49-9, Article 49 |
|---|---|
| Main Authors: | , |
| Format: | Article |
| Language: | English |
| Subjects: | |
| Citations: | Items that this one cites Items that cite this one |
| Online Access: | Get full text |
| Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
| cited_by | cdi_FETCH-LOGICAL-c409t-37d6c79b217d6076d666d49974cfc3ce403b09a4f057aab2a1b7c07339f6a9323 |
|---|---|
| cites | cdi_FETCH-LOGICAL-c409t-37d6c79b217d6076d666d49974cfc3ce403b09a4f057aab2a1b7c07339f6a9323 |
| container_end_page | 9 |
| container_issue | 4 |
| container_start_page | 49 |
| container_title | The European physical journal. E, Soft matter and biological physics |
| container_volume | 42 |
| creator | Charvolin, Jean Sadoc, Jean-François |
| description | .
The length of type-I collagen fibrils in solution increases through the development and progress of pointed tips appearing successively at the two ends of an axis-symmetric shaft with constant diameter. Those tips, respectively fine (
α
) or coarse (
β
) have opposite molecular orientations. The
α
-pointed tips, the first to appear, are particularly remarkable as they all show, on most of their length, a common parabolic profile which stays constant during the growth. Assuming that the latter occurs by lateral accretion of individual molecules in staggered configuration, we propose to give account of this prominent morphological feature along a purely geometrical argument, the profile of a tip being linked to the shape of the trajectories followed all along the accretion process. Among several possible trajectories, Fermat spirals lead to a parabolic profile in perfect agreement with the one observed for
α
-pointed tips. This is to be put in relation with the presence of such spirals in phyllotactic patterns which ensure the best packing efficiency in cases of axis-symmetry, which is indeed that of dense collagen fibrils. Moreover, those patterns are structured by concentric circles of dislocations, constitutive of the structure itself, whose behaviour might contribute to the mechanical properties of the fibrils.
Graphical abstract |
| doi_str_mv | 10.1140/epje/i2019-11812-1 |
| format | article |
| fullrecord | <record><control><sourceid>proquest_hal_p</sourceid><recordid>TN_cdi_hal_primary_oai_HAL_hal_04497509v1</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>2213151674</sourcerecordid><originalsourceid>FETCH-LOGICAL-c409t-37d6c79b217d6076d666d49974cfc3ce403b09a4f057aab2a1b7c07339f6a9323</originalsourceid><addsrcrecordid>eNp9kU9LAzEQxYMoWv98AQ-y4EUPazNJNmk8CKVYFQpeFLyFbDbbbtlt1qRV-u3NtlrBg6cMye_NvMlD6BzwDQDDfdvObb8iGGQKMACSwh7qAZEkHcjsbX9XMzhCxyHMMcZRRg_REQUcFRnvobuXdWvTp8S4utZTu0jKKvdVHW6TsXdNMvXuczlLGufbmavddJ0sXVI7o-vE-cL6U3RQ6jrYs-_zBL2O719Gj-nk-eFpNJykhmG5TKkouBEyJxALLHjBOS-YlIKZ0lBjo6scS81KnAmtc6IhFwYLSmXJtaSEnqDrbd-ZrlXrq0b7tXK6Uo_DieruMGNSZFh-QGSvtmzr3fvKhqVqqmBs3G9h3SooQoBCBlywiF7-Qedu5Rdxk44ignNKcKTIljLeheBtuXMAWHVJqC4JtUlCbZJQnYuL79arvLHFTvLz9RGgWyDEp8XU-t_Z_7T9AtgdksA</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>2212766320</pqid></control><display><type>article</type><title>Type-I collagen fibrils: From growth morphology to local order</title><source>Springer Nature</source><creator>Charvolin, Jean ; Sadoc, Jean-François</creator><creatorcontrib>Charvolin, Jean ; Sadoc, Jean-François</creatorcontrib><description>.
The length of type-I collagen fibrils in solution increases through the development and progress of pointed tips appearing successively at the two ends of an axis-symmetric shaft with constant diameter. Those tips, respectively fine (
α
) or coarse (
β
) have opposite molecular orientations. The
α
-pointed tips, the first to appear, are particularly remarkable as they all show, on most of their length, a common parabolic profile which stays constant during the growth. Assuming that the latter occurs by lateral accretion of individual molecules in staggered configuration, we propose to give account of this prominent morphological feature along a purely geometrical argument, the profile of a tip being linked to the shape of the trajectories followed all along the accretion process. Among several possible trajectories, Fermat spirals lead to a parabolic profile in perfect agreement with the one observed for
α
-pointed tips. This is to be put in relation with the presence of such spirals in phyllotactic patterns which ensure the best packing efficiency in cases of axis-symmetry, which is indeed that of dense collagen fibrils. Moreover, those patterns are structured by concentric circles of dislocations, constitutive of the structure itself, whose behaviour might contribute to the mechanical properties of the fibrils.
Graphical abstract</description><identifier>ISSN: 1292-8941</identifier><identifier>EISSN: 1292-895X</identifier><identifier>DOI: 10.1140/epje/i2019-11812-1</identifier><identifier>PMID: 31011856</identifier><language>eng</language><publisher>Berlin/Heidelberg: Springer Berlin Heidelberg</publisher><subject>Biological and Medical Physics ; Biophysics ; Collagen ; Collagen Type I - chemistry ; Complex Fluids and Microfluidics ; Complex Systems ; Condensed matter physics ; Deposition ; Dislocations ; Mathematical morphology ; Mechanical properties ; Models, Molecular ; Nanotechnology ; Physics ; Physics and Astronomy ; Polymer Sciences ; Protein Conformation, alpha-Helical ; Regular Article ; Soft and Granular Matter ; Spirals ; Staggered configuration ; Surfaces and Interfaces ; Symmetry ; Thin Films ; Tips ; Trajectories</subject><ispartof>The European physical journal. E, Soft matter and biological physics, 2019-04, Vol.42 (4), p.49-9, Article 49</ispartof><rights>EDP Sciences, Società Italiana di Fisica and Springer-Verlag GmbH Germany, part of Springer Nature 2019</rights><rights>Copyright Springer Nature B.V. 2019</rights><rights>Distributed under a Creative Commons Attribution 4.0 International License</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c409t-37d6c79b217d6076d666d49974cfc3ce403b09a4f057aab2a1b7c07339f6a9323</citedby><cites>FETCH-LOGICAL-c409t-37d6c79b217d6076d666d49974cfc3ce403b09a4f057aab2a1b7c07339f6a9323</cites><orcidid>0000-0002-3332-244X</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>230,314,780,784,885,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/31011856$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://hal.science/hal-04497509$$DView record in HAL$$Hfree_for_read</backlink></links><search><creatorcontrib>Charvolin, Jean</creatorcontrib><creatorcontrib>Sadoc, Jean-François</creatorcontrib><title>Type-I collagen fibrils: From growth morphology to local order</title><title>The European physical journal. E, Soft matter and biological physics</title><addtitle>Eur. Phys. J. E</addtitle><addtitle>Eur Phys J E Soft Matter</addtitle><description>.
The length of type-I collagen fibrils in solution increases through the development and progress of pointed tips appearing successively at the two ends of an axis-symmetric shaft with constant diameter. Those tips, respectively fine (
α
) or coarse (
β
) have opposite molecular orientations. The
α
-pointed tips, the first to appear, are particularly remarkable as they all show, on most of their length, a common parabolic profile which stays constant during the growth. Assuming that the latter occurs by lateral accretion of individual molecules in staggered configuration, we propose to give account of this prominent morphological feature along a purely geometrical argument, the profile of a tip being linked to the shape of the trajectories followed all along the accretion process. Among several possible trajectories, Fermat spirals lead to a parabolic profile in perfect agreement with the one observed for
α
-pointed tips. This is to be put in relation with the presence of such spirals in phyllotactic patterns which ensure the best packing efficiency in cases of axis-symmetry, which is indeed that of dense collagen fibrils. Moreover, those patterns are structured by concentric circles of dislocations, constitutive of the structure itself, whose behaviour might contribute to the mechanical properties of the fibrils.
Graphical abstract</description><subject>Biological and Medical Physics</subject><subject>Biophysics</subject><subject>Collagen</subject><subject>Collagen Type I - chemistry</subject><subject>Complex Fluids and Microfluidics</subject><subject>Complex Systems</subject><subject>Condensed matter physics</subject><subject>Deposition</subject><subject>Dislocations</subject><subject>Mathematical morphology</subject><subject>Mechanical properties</subject><subject>Models, Molecular</subject><subject>Nanotechnology</subject><subject>Physics</subject><subject>Physics and Astronomy</subject><subject>Polymer Sciences</subject><subject>Protein Conformation, alpha-Helical</subject><subject>Regular Article</subject><subject>Soft and Granular Matter</subject><subject>Spirals</subject><subject>Staggered configuration</subject><subject>Surfaces and Interfaces</subject><subject>Symmetry</subject><subject>Thin Films</subject><subject>Tips</subject><subject>Trajectories</subject><issn>1292-8941</issn><issn>1292-895X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2019</creationdate><recordtype>article</recordtype><recordid>eNp9kU9LAzEQxYMoWv98AQ-y4EUPazNJNmk8CKVYFQpeFLyFbDbbbtlt1qRV-u3NtlrBg6cMye_NvMlD6BzwDQDDfdvObb8iGGQKMACSwh7qAZEkHcjsbX9XMzhCxyHMMcZRRg_REQUcFRnvobuXdWvTp8S4utZTu0jKKvdVHW6TsXdNMvXuczlLGufbmavddJ0sXVI7o-vE-cL6U3RQ6jrYs-_zBL2O719Gj-nk-eFpNJykhmG5TKkouBEyJxALLHjBOS-YlIKZ0lBjo6scS81KnAmtc6IhFwYLSmXJtaSEnqDrbd-ZrlXrq0b7tXK6Uo_DieruMGNSZFh-QGSvtmzr3fvKhqVqqmBs3G9h3SooQoBCBlywiF7-Qedu5Rdxk44ignNKcKTIljLeheBtuXMAWHVJqC4JtUlCbZJQnYuL79arvLHFTvLz9RGgWyDEp8XU-t_Z_7T9AtgdksA</recordid><startdate>20190418</startdate><enddate>20190418</enddate><creator>Charvolin, Jean</creator><creator>Sadoc, Jean-François</creator><general>Springer Berlin Heidelberg</general><general>Springer Nature B.V</general><general>EDP Sciences: EPJ</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope><scope>1XC</scope><orcidid>https://orcid.org/0000-0002-3332-244X</orcidid></search><sort><creationdate>20190418</creationdate><title>Type-I collagen fibrils: From growth morphology to local order</title><author>Charvolin, Jean ; Sadoc, Jean-François</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c409t-37d6c79b217d6076d666d49974cfc3ce403b09a4f057aab2a1b7c07339f6a9323</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2019</creationdate><topic>Biological and Medical Physics</topic><topic>Biophysics</topic><topic>Collagen</topic><topic>Collagen Type I - chemistry</topic><topic>Complex Fluids and Microfluidics</topic><topic>Complex Systems</topic><topic>Condensed matter physics</topic><topic>Deposition</topic><topic>Dislocations</topic><topic>Mathematical morphology</topic><topic>Mechanical properties</topic><topic>Models, Molecular</topic><topic>Nanotechnology</topic><topic>Physics</topic><topic>Physics and Astronomy</topic><topic>Polymer Sciences</topic><topic>Protein Conformation, alpha-Helical</topic><topic>Regular Article</topic><topic>Soft and Granular Matter</topic><topic>Spirals</topic><topic>Staggered configuration</topic><topic>Surfaces and Interfaces</topic><topic>Symmetry</topic><topic>Thin Films</topic><topic>Tips</topic><topic>Trajectories</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Charvolin, Jean</creatorcontrib><creatorcontrib>Sadoc, Jean-François</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><collection>Hyper Article en Ligne (HAL)</collection><jtitle>The European physical journal. E, Soft matter and biological physics</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Charvolin, Jean</au><au>Sadoc, Jean-François</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Type-I collagen fibrils: From growth morphology to local order</atitle><jtitle>The European physical journal. E, Soft matter and biological physics</jtitle><stitle>Eur. Phys. J. E</stitle><addtitle>Eur Phys J E Soft Matter</addtitle><date>2019-04-18</date><risdate>2019</risdate><volume>42</volume><issue>4</issue><spage>49</spage><epage>9</epage><pages>49-9</pages><artnum>49</artnum><issn>1292-8941</issn><eissn>1292-895X</eissn><abstract>.
The length of type-I collagen fibrils in solution increases through the development and progress of pointed tips appearing successively at the two ends of an axis-symmetric shaft with constant diameter. Those tips, respectively fine (
α
) or coarse (
β
) have opposite molecular orientations. The
α
-pointed tips, the first to appear, are particularly remarkable as they all show, on most of their length, a common parabolic profile which stays constant during the growth. Assuming that the latter occurs by lateral accretion of individual molecules in staggered configuration, we propose to give account of this prominent morphological feature along a purely geometrical argument, the profile of a tip being linked to the shape of the trajectories followed all along the accretion process. Among several possible trajectories, Fermat spirals lead to a parabolic profile in perfect agreement with the one observed for
α
-pointed tips. This is to be put in relation with the presence of such spirals in phyllotactic patterns which ensure the best packing efficiency in cases of axis-symmetry, which is indeed that of dense collagen fibrils. Moreover, those patterns are structured by concentric circles of dislocations, constitutive of the structure itself, whose behaviour might contribute to the mechanical properties of the fibrils.
Graphical abstract</abstract><cop>Berlin/Heidelberg</cop><pub>Springer Berlin Heidelberg</pub><pmid>31011856</pmid><doi>10.1140/epje/i2019-11812-1</doi><tpages>9</tpages><orcidid>https://orcid.org/0000-0002-3332-244X</orcidid></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 1292-8941 |
| ispartof | The European physical journal. E, Soft matter and biological physics, 2019-04, Vol.42 (4), p.49-9, Article 49 |
| issn | 1292-8941 1292-895X |
| language | eng |
| recordid | cdi_hal_primary_oai_HAL_hal_04497509v1 |
| source | Springer Nature |
| subjects | Biological and Medical Physics Biophysics Collagen Collagen Type I - chemistry Complex Fluids and Microfluidics Complex Systems Condensed matter physics Deposition Dislocations Mathematical morphology Mechanical properties Models, Molecular Nanotechnology Physics Physics and Astronomy Polymer Sciences Protein Conformation, alpha-Helical Regular Article Soft and Granular Matter Spirals Staggered configuration Surfaces and Interfaces Symmetry Thin Films Tips Trajectories |
| title | Type-I collagen fibrils: From growth morphology to local order |
| url | http://sfxeu10.hosted.exlibrisgroup.com/loughborough?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-04T02%3A46%3A27IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_hal_p&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Type-I%20collagen%20fibrils:%20From%20growth%20morphology%20to%20local%20order&rft.jtitle=The%20European%20physical%20journal.%20E,%20Soft%20matter%20and%20biological%20physics&rft.au=Charvolin,%20Jean&rft.date=2019-04-18&rft.volume=42&rft.issue=4&rft.spage=49&rft.epage=9&rft.pages=49-9&rft.artnum=49&rft.issn=1292-8941&rft.eissn=1292-895X&rft_id=info:doi/10.1140/epje/i2019-11812-1&rft_dat=%3Cproquest_hal_p%3E2213151674%3C/proquest_hal_p%3E%3Cgrp_id%3Ecdi_FETCH-LOGICAL-c409t-37d6c79b217d6076d666d49974cfc3ce403b09a4f057aab2a1b7c07339f6a9323%3C/grp_id%3E%3Coa%3E%3C/oa%3E%3Curl%3E%3C/url%3E&rft_id=info:oai/&rft_pqid=2212766320&rft_id=info:pmid/31011856&rfr_iscdi=true |