A fractal nature for polymerized laminin.

Polylaminin (polyLM) is a non-covalent acid-induced nano- and micro-structured polymer of the protein laminin displaying distinguished biological properties. Polylaminin stimulates neuritogenesis beyond the levels achieved by ordinary laminin and has been shown to promote axonal regeneration in anim...

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Main Authors: Camila Hochman-Mendez, Marco Cantini, David Moratal, Manuel Salmeron-Sanchez, Tatiana Coelho-Sampaio
Format: Article
Language:English
Published: Public Library of Science (PLoS) 2014-01-01
Series:PLoS ONE
Online Access:https://doi.org/10.1371/journal.pone.0109388
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spelling doaj-b4731583d9ba42b18149dfbdacade0512021-03-04T08:54:23ZengPublic Library of Science (PLoS)PLoS ONE1932-62032014-01-01910e10938810.1371/journal.pone.0109388A fractal nature for polymerized laminin.Camila Hochman-MendezMarco CantiniDavid MoratalManuel Salmeron-SanchezTatiana Coelho-SampaioPolylaminin (polyLM) is a non-covalent acid-induced nano- and micro-structured polymer of the protein laminin displaying distinguished biological properties. Polylaminin stimulates neuritogenesis beyond the levels achieved by ordinary laminin and has been shown to promote axonal regeneration in animal models of spinal cord injury. Here we used confocal fluorescence microscopy (CFM), scanning electron microscopy (SEM) and atomic force microscopy (AFM) to characterize its three-dimensional structure. Renderization of confocal optical slices of immunostained polyLM revealed the aspect of a loose flocculated meshwork, which was homogeneously stained by the antibody. On the other hand, an ordinary matrix obtained upon adsorption of laminin in neutral pH (LM) was constituted of bulky protein aggregates whose interior was not accessible to the same anti-laminin antibody. SEM and AFM analyses revealed that the seed unit of polyLM was a flat polygon formed in solution whereas the seed structure of LM was highly heterogeneous, intercalating rod-like, spherical and thin spread lamellar deposits. As polyLM was visualized at progressively increasing magnifications, we observed that the morphology of the polymer was alike independently of the magnification used for the observation. A search for the Hausdorff dimension in images of the two matrices showed that polyLM, but not LM, presented fractal dimensions of 1.55, 1.62 and 1.70 after 1, 8 and 12 hours of adsorption, respectively. Data in the present work suggest that the intrinsic fractal nature of polymerized laminin can be the structural basis for the fractal-like organization of basement membranes in the neurogenic niches of the central nervous system.https://doi.org/10.1371/journal.pone.0109388
collection DOAJ
language English
format Article
sources DOAJ
author Camila Hochman-Mendez
Marco Cantini
David Moratal
Manuel Salmeron-Sanchez
Tatiana Coelho-Sampaio
spellingShingle Camila Hochman-Mendez
Marco Cantini
David Moratal
Manuel Salmeron-Sanchez
Tatiana Coelho-Sampaio
A fractal nature for polymerized laminin.
PLoS ONE
author_facet Camila Hochman-Mendez
Marco Cantini
David Moratal
Manuel Salmeron-Sanchez
Tatiana Coelho-Sampaio
author_sort Camila Hochman-Mendez
title A fractal nature for polymerized laminin.
title_short A fractal nature for polymerized laminin.
title_full A fractal nature for polymerized laminin.
title_fullStr A fractal nature for polymerized laminin.
title_full_unstemmed A fractal nature for polymerized laminin.
title_sort fractal nature for polymerized laminin.
publisher Public Library of Science (PLoS)
series PLoS ONE
issn 1932-6203
publishDate 2014-01-01
description Polylaminin (polyLM) is a non-covalent acid-induced nano- and micro-structured polymer of the protein laminin displaying distinguished biological properties. Polylaminin stimulates neuritogenesis beyond the levels achieved by ordinary laminin and has been shown to promote axonal regeneration in animal models of spinal cord injury. Here we used confocal fluorescence microscopy (CFM), scanning electron microscopy (SEM) and atomic force microscopy (AFM) to characterize its three-dimensional structure. Renderization of confocal optical slices of immunostained polyLM revealed the aspect of a loose flocculated meshwork, which was homogeneously stained by the antibody. On the other hand, an ordinary matrix obtained upon adsorption of laminin in neutral pH (LM) was constituted of bulky protein aggregates whose interior was not accessible to the same anti-laminin antibody. SEM and AFM analyses revealed that the seed unit of polyLM was a flat polygon formed in solution whereas the seed structure of LM was highly heterogeneous, intercalating rod-like, spherical and thin spread lamellar deposits. As polyLM was visualized at progressively increasing magnifications, we observed that the morphology of the polymer was alike independently of the magnification used for the observation. A search for the Hausdorff dimension in images of the two matrices showed that polyLM, but not LM, presented fractal dimensions of 1.55, 1.62 and 1.70 after 1, 8 and 12 hours of adsorption, respectively. Data in the present work suggest that the intrinsic fractal nature of polymerized laminin can be the structural basis for the fractal-like organization of basement membranes in the neurogenic niches of the central nervous system.
url https://doi.org/10.1371/journal.pone.0109388
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