Collagen structure and functional implications

Ottani, Vittoria; Raspanti, Mario; Ruggeri, Alessandro

doi:10.1016/s0968-4328(00)00042-1

Cited by 361 publications

(305 citation statements)

References 59 publications

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“…The integrity of the collagen molecule is attributed to the formation of intra-and intermolecular cross-linking which contribute to the mechanical strength of the bone organic matrix (Eyre & Wu, 2005;Ottani et al, 2001;Saito & Marumo, 2009). Inter-molecular collagen cross-links can be divided into two types: lysine hydroxylase/lysyl oxidasecontrolled cross-links (enzymatic cross-links) and glycation/oxidation-induced cross-links.…”

Section: Organic Phasementioning

confidence: 99%

“…Moreover, each structural level may undergo minor but fundamental modifications, to better adapt and respond to various biomechanical forces (Ottani et al, 2001). As stated in a basic rule of skeletal biology known as Wolff´s law, "the bone´s morphology is a reflection of what function the bone has been built to do or adapted to perform".…”

Section: Bone Matrix Structurementioning

confidence: 99%

See 1 more Smart Citation

Characterization of Bone and Bone-Based Graft Materials Using FTIR Spectroscopy

Figueiredo¹,

Gamelas²,

Martins³

2012

Infrared Spectroscopy - Life and Biomedical Sciences

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Section: Organic Phasementioning

confidence: 99%

Section: Bone Matrix Structurementioning

confidence: 99%

Characterization of Bone and Bone-Based Graft Materials Using FTIR Spectroscopy

Figueiredo¹,

Gamelas²,

Martins³

2012

Infrared Spectroscopy - Life and Biomedical Sciences

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“…16 obtained from the oldest patient (age 71 years). The shape, size and appearance of these rods strikingly resemble the building units derived from collagen fibres, consisting of 40 nm wide and 300 nm long [11]. These rods could derive from collagen fibres that disintegrated into individual building units (macromolecules) with some showing further breakdown into smaller fragments because of physical activity.…”

Section: Discussionmentioning

confidence: 91%

Ultrafine Structure of Calcific Deposits Developed in Calcific Tendinopathy

Zelenková¹,

Söhnel²,

Gráses³

2015

JBPC

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The ultrafine structure of tendons deposits formed in three patients, males aged 52 and 61 years and a female aged 71 years were evaluated by atomic force microscopy. Three distinctly different structures of deposit surface were identified: (i) compact, smooth and uneven surface composed of closely packed nanoparticles of diameter 30 nm; (ii) surfaces consisting of plate-like crystalline particles about 30 nm thick that formed larger entities divided by deep depressions; (iii) rough surface formed by individual or closely attached elongated needle-like particles with elliptical cross-section of diameter about 30 nm. These surface structures were developed by different formation mechanisms: (i) Aggregation of Posner's clusters into nanoparticles formed on biological calcific able surfaces and in the bulk of body fluid surrounding the deposits that subsequently settled onto the deposit surface; (ii) Regular crystal growth on surface nuclei generated at low supersaturation of body fluid with respect to the phosphatic phase and/or in a narrow cavity containing a very limited volume of liquid; (iii) Solution mediated re-crystallization of the upper layers of a deposit or unstable crystalline growth governed by volume diffusion of building units to the particle tip. Small rods, 40 nm wide and from 100 to 300 nm long, with no apparent order were detected only on the surface of deposit formed in the female patient. These rods could be debris of collagen fibres that disintegrated into individual building units (macromolecules) with some showing breakdown into smaller fragments.

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“…The structure and properties of the triple helix molecule in type I collagen is an area of intense investigation because the interactions between collagen, mineral bioceramics, and their surrounding environment are important to many bio-related systems. Collagen is a complex multifunctional protein whose various forms are based on different amino acid (residue) sequences contained therein [2][3][4][5]. The most abundant collagen, type I, has a long rod-like triple helix structure [4,6] consisting of three intertwined polypeptide chains, called α-chains, of approximately 3000 Å in length and 15 Å in diameter.…”

Section: Introductionmentioning

confidence: 99%

“…Collagen is a complex multifunctional protein whose various forms are based on different amino acid (residue) sequences contained therein [2][3][4][5]. The most abundant collagen, type I, has a long rod-like triple helix structure [4,6] consisting of three intertwined polypeptide chains, called α-chains, of approximately 3000 Å in length and 15 Å in diameter. Most type I collagen is in the heterotrimer [α1(I)] 2 [α2(I)] form, where α1(I) and α2(I) are polypeptide chains.…”

Section: Introductionmentioning

confidence: 99%

Computational Study of a Heterostructural Model of Type I Collagen and Implementation of an Amino Acid Potential Method Applicable to Large Proteins

et al. 2014

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Collagen molecules are the primary structural proteins of many biological systems. Much progress has been made in the study of the structure and function of collagen, but fundamental understanding of its electronic structures at the atomic level is still lacking. We present the results of electronic structure and bonding calculations of a specific model of type I collagen using the density functional theory-based method. Information on density of states (DOS), partial DOS, effective charges, bond order values, and intra-and inter-molecular H-bonding are obtained and discussed. We further devised an amino-acid-based potential method (AAPM) to circumvent the full self-consistent field (SCF) calculation that can be applied to large proteins. The AAPM is validated by comparing the results with the full SCF calculation of the whole type I collagen model with three strands. The calculated effective charges on each atom in the model retained at least 95% accuracy. This technique provides a viable and efficient way to study the electronic structure of large complex biomaterials at the ab initio level.

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Collagen structure and functional implications

Cited by 361 publications

References 59 publications

Characterization of Bone and Bone-Based Graft Materials Using FTIR Spectroscopy

Characterization of Bone and Bone-Based Graft Materials Using FTIR Spectroscopy

Ultrafine Structure of Calcific Deposits Developed in Calcific Tendinopathy

Computational Study of a Heterostructural Model of Type I Collagen and Implementation of an Amino Acid Potential Method Applicable to Large Proteins

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