Effects of various salts on structural polymorphism of reconstituted type I collagen fibrils

Li, Yuping; Douglas, Elliot P.

doi:10.1016/j.colsurfb.2013.07.037

Cited by 65 publications

(61 citation statements)

References 60 publications

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“…The third step is a plateau phase where turbidity stops increasing, suggesting the formation of the three-dimensional networks of fibrils (Sai & Babu, 2001;Zhang et al, 2014b). The fibril-forming rate of ASC-P and PSC-P was more rapid than that of ASC-G and PSC-G. Additionally, ASCs exhibited a slightly rapid rise in turbidity than their corresponding PSCs, since the telopeptide regions at the N-and C-termini are important in stabilizing initial aggregates, enzymatic digestion of the telopeptide regions might inhibit the fibril formation process (Li & Douglas, 2013). …”

Section: Fibril-forming Ability In Vitromentioning

confidence: 99%

“…The average D-periodicity of ASC-G (66.90 ± 2.35 nm) and PSC-G (66.88 ± 2.17 nm) was slightly smaller than that of ASC-P (67.95 ± 2.07 nm) and PSC-P (67.58 ± 1.89 nm) (p > 0.05). Studies have shown that D-periodicity served as an indication for the reconstruction of native-like fibrils which are important in maintaining mechanical stability and biological functions of load-bearing materials (Li & Douglas, 2013). Fibrils with native D-periodicity also play an important role in mineralization by providing structure templates where minerals are deposited in the gap zones of fibrils (Nudelman et al, 2010).…”

Section: Tem Observation Of Fibrilsmentioning

confidence: 99%

“…Fibril samples were loaded on 200 mesh copper grids and stained with 1% phosphotungstic acid (Li & Douglas, 2013). TEM images were observed using a transmission electron microscopy (JSM-1200, JEDL Ltd., Tokyo, Japan).…”

Section: Transmission Electron Microscopy (Tem)mentioning

confidence: 99%

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Physicochemical characteristics and fibril-forming properties of collagen from paddlefish (Polyodon spathula) and globefish (Fugu flavidus) skin byproducts

2017

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Acid-soluble collagen (ASC) and pepsin-soluble collagen (PSC) from the skin byproducts of paddlefish (ASC-P and PSC-P) and globefish (ASC-G and PSC-G) were purified and characterized. The imino acid contents of ASC-P, PSC-P, 197.9, 186.4 and 189.7 residues/1000 residues, respectively. SDS-polyacrylamide gel electrophoresis (SDS-PAGE) and Fourier transform infrared spectroscopy (FTIR) confirmed that all four samples composed of two different α1-and α2-chains with integrated triple-helical structure. Denaturation temperatures of ASC-P, PSC-P, ASC-G and PSC-G were 29.6, 28.2, 27.4 and 26.9 °C, respectively. Based on Transmission electron microscopy (TEM) observation, all four samples could assemble into fibrils in vitro with D-periodicity. However, the fibril-forming rate of ASC-P and PSC-P was more rapid than that of ASC-G and PSC-G. Scanning electron microscopy (SEM) analysis confirmed well-defined fibril morphologies,the diameter of fibrils from ASC-P and PSC-P was thicker than those of ASC-G and PSC-G after 24 h incubation. These results indicated that paddlefish and globefish skin collagens could be alternatives to terrestrial collagens for applications in food-packaging, nutraceutical and pharmaceutical industries.Keywords: paddlefish; globefish; collagen; physicochemical property; fibril-forming property; fibril morphology.Practical Application: Utilization of paddlefish and globefish skin byproducts by extracting collagen with good physicochemical and fibril-forming properties.

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Section: Fibril-forming Ability In Vitromentioning

confidence: 99%

Section: Tem Observation Of Fibrilsmentioning

confidence: 99%

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Physicochemical characteristics and fibril-forming properties of collagen from paddlefish (Polyodon spathula) and globefish (Fugu flavidus) skin byproducts

2017

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“…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). The various stages of collagen assembly can be isolated and studied independently by manipulating the solution conditions.…”

Section: Introductionmentioning

confidence: 99%

“…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%

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

Drzewiecki

Grisham

Parmar

et al. 2016

Biophysical Journal

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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.

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Biotechnological Valorization of Marine Collagens

Fassini

Oliveira

Silva

et al. 2020

Encyclopedia of Marine Biotechnology

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Effects of various salts on structural polymorphism of reconstituted type I collagen fibrils

Cited by 65 publications

References 60 publications

Physicochemical characteristics and fibril-forming properties of collagen from paddlefish (Polyodon spathula) and globefish (Fugu flavidus) skin byproducts

Physicochemical characteristics and fibril-forming properties of collagen from paddlefish (Polyodon spathula) and globefish (Fugu flavidus) skin byproducts

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

Biotechnological Valorization of Marine Collagens

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