In vitro fibrillogenesis of collagen type I in varying ionic and pH conditions

Harris, J. Robin; Soliakov, Andrei; Lewis, Richard J.

doi:10.1016/j.micron.2013.03.004

Cited by 99 publications

(107 citation statements)

References 42 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…This means that the dialysis stage removed salts and acids until the samples achieve an average pH value of 6.3, no matter what the extraction method was. At this pH value, the collagen molecules tend to form little fibres (Harris & Reiber, 2007;Harris, Soliakov, & Lewis, 2013;Li, Asadi, Monroe, & Douglas, 2009). These results suggest that collagen obtained from rabbit skins could be used in the cosmetology industry as the obtained pH value is closer to the neutral pH values.…”

Section: Phmentioning

confidence: 99%

Extraction and characterization of collagen from rabbit skin: partial characterization

Martínez-Ortiz

Hernández-Fuentes

Pimentel-González

et al. 2014

CyTA - Journal of Food

View full text Add to dashboard Cite

(2015) Extraction and characterization of collagen from rabbit skin: partial characterization, CyTAJournal of Food, 13:2, 253-258, DOI: 10.1080/19476337.2014 To link to this article: https://doi.org/10. 1080/19476337.2014 Extraction and characterization of collagen were carried out in rabbit skins as a new alternative for collagen type I. Acetic acid and pepsin were for the extraction of soluble and insoluble collagen, respectively. The enzymatic treatment yielded higher amount of collagen (71%). The average pH value was 6.3, no matter what the method of extraction was. Denaturation temperature of collagen was found at 36°C approximately in two different techniques: Rheometer and Differential Scanning Calorimetry (DSC). Despite the amount of collagen in solution was low, its viscosity was high because of the hydrodynamic behaviour of collagen molecules. Sodium dodecyl sulphate polyacrylamide gel electrophoresis results showed three different bands that reflected two alpha-chains and one beta-chain with molecular weights of 102, 118 and 220 kDa, respectively. Determination of hydroxyproline gave evidence that the extracted material was collagen. It was concluded that rabbit skin could be an alternative source for the extraction of collagen.Keywords: collagen; rabbit skin; extraction; thermal analysis Se realizó la extracción y caracterización de colágeno en pieles de conejo como una nueva alternativa para colágeno tipo I. Se usaron ácido acético y pepsina para la extracción de colágeno soluble e insoluble respectivamente. El tratamiento enzimático fue el que rindió alta cantidad de colágeno (71%). El pH promedio fue de 6,3 sin importar cuál fue el método de extracción. La temperatura de desnaturalización del colágeno se encontró a 36°C aproximadamente mediante dos diferentes técnicas: Reometría y DSC. A pesar de que la cantidad de colágeno en la solución fue bajo, su viscosidad fue alta debido a el comportamiento hidrodinámico de las moléculas. Los resultados de SDS-PAGE mostraron tres diferentes bandas en las que se reflejaron dos cadenas alfa y una cadena beta con pesos moleculares de 102, 118 and 220 kDa respectivamente. La determinación del contenido de hidroxiprolina dio evidencia de que el material extraído fue colágeno. Se concluyó que la piel de conejo podría ser una alternativa de materia prima para la extracción de colágeno.

show abstract

Section: Phmentioning

confidence: 99%

Extraction and characterization of collagen from rabbit skin: partial characterization

Martínez-Ortiz

Hernández-Fuentes

Pimentel-González

et al. 2014

CyTA - Journal of Food

View full text Add to dashboard Cite

show abstract

“…However, many of the structural and functional features of assembled fibrils can be recreated in vitro under appropriate conditions using collagen extracted from a variety of source animal tissues into neutral salt or buffers, or, more frequently, into dilute acidic solutions (1). Fibrillogenesis can be controlled by varying the pH (17)(18)(19)(20), temperature (18,19,21,22), and buffer conditions (17,18,23,24). Under acidic conditions, collagen exists primarily as a soluble triple helix (17) below its melting transition around 42 C (24).…”

Section: Introductionmentioning

confidence: 99%

“…Fibrillogenesis can be controlled by varying the pH (17)(18)(19)(20), temperature (18,19,21,22), and buffer conditions (17,18,23,24). Under acidic conditions, collagen exists primarily as a soluble triple helix (17) below its melting transition around 42 C (24). At neutral pH, collagen readily forms fibrils above 20 C (17).…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Circular Dichroism Spectroscopy of Collagen Fibrillogenesis: A New Use for an Old Technique

Drzewiecki

Grisham

Parmar

et al. 2016

Biophysical Journal

View full text Add to dashboard Cite

Type-I collagen assembles in a stepwise, hierarchic fashion from the folding of the triple helix to the assembly of fibrils into fibers. The mature assembled fibers are crucial for tissue structure and mechanics, cell interactions, and other functions in vivo. Although triple helix folding can be followed with the use of optical methods such as circular dichroism (CD) spectroscopy, fibrillogenesis is typically measured by alternative methods such as turbidity, rheology, and microscopy. Together, these approaches allow for investigation of the mechanical properties and architectures of collagen-based scaffolds and excised tissues. Herein, we demonstrate that CD spectroscopy, a technique that is used primarily to evaluate the secondary structure of proteins, can also be employed to monitor collagen fibrillogenesis. Type-I collagen suspensions demonstrated a strong, negative ellipticity band between 204 and 210 nm under conditions consistent with fibrillogenesis. Deconvolution of CD spectra before, during, and after fibrillogenesis identified a unique fibril spectrum distinct from triple helix and random coil conformations. The ability to monitor multiple states of collagen simultaneously in one experiment using one modality provides a powerful platform for studying this complex assembly process and the effects of other factors, such as collagenases, on fibrillogenesis and degradation.

show abstract

“…With the exception of shore hardness the biological additions made no significant difference This range of pH values is conducive for the collagen Type I addition to form molecular aggregates, fibrils and ultimately fibres (29). Previously the formation of 70 ̴ nm collagen granules upon glass ionomers has been observed in SEM and AFM studies (30).…”

mentioning

confidence: 95%

Investigating the addition of collagen and its integrin binding sequence (RGD) to glass polyalkenoate: In terms of material and cellular properties to explore a more biocompatible method of root caries restoration

Salem

Jones

Ellis

et al. 2016

Journal of Dentistry

View full text Add to dashboard Cite

In vitro fibrillogenesis of collagen type I in varying ionic and pH conditions

Cited by 99 publications

References 42 publications

Extraction and characterization of collagen from rabbit skin: partial characterization

Extraction and characterization of collagen from rabbit skin: partial characterization

Circular Dichroism Spectroscopy of Collagen Fibrillogenesis: A New Use for an Old Technique

Investigating the addition of collagen and its integrin binding sequence (RGD) to glass polyalkenoate: In terms of material and cellular properties to explore a more biocompatible method of root caries restoration

Contact Info

Product

Resources

About