Evidence of a Discrete Axial Structure in Unimodal Collagen Fibrils

• Published in: Biomacromolecules Vol. 12; no. 12; pp. 4344 - 4347
• Main Authors: Raspanti, Mario, Reguzzoni, Marcella, Protasoni, Marina, Martini, Désirée
• Format: Journal Article
• Language: English
• Published: Washington, DC American Chemical Society 12.12.2011
• Subjects: Animals; Biological and medical sciences; Central Nervous System - chemistry; Collagen - chemistry; Collagen - ultrastructure; Connective Tissue; Extracellular Matrix; Fundamental and applied biological sciences. Psychology; Microfibrils; Microscopy, Atomic Force - methods; Microscopy, Electron; Molecular biophysics; Rabbits; Structure in molecular biology; Supramolecular structure; Tendons - chemistry; Vertebrata; Farming animal; Mammalia; Architecture; Collagen; Supramolecular structure; Glycoprotein; Rabbit; Lagomorpha; Fibril
• ISSN: 1525-7797; 1526-4602
• DOI: 10.1021/bm201314e

The collagen fibrils of cornea, blood vessel walls, skin, gut, interstitial tissues, the sheath of tendons and nerves, and other connective tissues are known to be made of helically wound subfibrils winding at a constant angle to the fibril axis. A critical aspect of this model is that it requires the axial microfibrils to warp in an implausible way. This architecture lends itself quite naturally to an epitaxial layout where collagen microfibrils envelop a central core of a different nature. Here we demonstrate an axial domain in collagen fibrils from rabbit nerve sheath and tendon sheath by means of transmission electron microscopy after a histochemical reaction designed to evidence all polysaccharides and by tapping-mode atomic force microscopy. This axial domain was consistently found in fibrils with helical microfibrils but was not observed in tendon, whose microfibrils run longitudinal and parallel.