Hierarchical assembly and the onset of banding in fibrous long spacing collagen revealed by atomic force microscopy

Rainey, Jan K.; Wen, Chuck K.; Goh, M. Cynthia

doi:10.1016/s0945-053x(02)00101-4

Cited by 31 publications

(19 citation statements)

References 51 publications

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“…Actually, in an assembly process either in vivo or in vitro, there are many other molecules, such as hyaluronic acid and chondroitin sulfate in co-existence of that might all contribute to the ultimate kinetics in different ways. In fact, it is not surprising to see that kinetics studies of type I collagen assembly in co-existing with those molecules have become subjects of interest lately and some initial results seem to be quite encouraging [28][29][30]. We hope that by studying the roles played by those molecules in the kinetics of type II collagen assembly in vitro would be eventually helpful in the formulation of some proper ECM material.…”

Section: Resultsmentioning

confidence: 98%

Influences of hyaluronan on type II collagen fibrillogenesis in vitro

Kuo

Wang²,

Niu

et al. 2007

J Mater Sci: Mater Med

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The effect to the kinetics of type II collagen fibrillogenesis with the addition of hyaluronan (HA), (M w of 1.8 · 10 6 Da), at various concentrations of HA (0.01, 0.05 and 0.1 wt.%) for a series of fibril formation systems was examined in this study. Evidences deduced from the turbidity-time curves revealed that the inclusion of HA had minor or no impact to the fibrillogenesis of type II collagen (collagen conc. at 0.2 mg/mL). The apparent rate constants, k lag (lag phase) increased slightly but k g (growth phase) decreased not very significantly with addition of HA, as compared to the case of pure collagen. This leads us to believe tentatively that, with the addition of HA to collagen solutions, the nucleation process of the fibril formation might have been sped up slightly whereas the growth process slowed up slightly. However, data from TEM observations on the resulting fibrils indicated that the presence of HA did not significantly affect the diameters and the characteristic D-banding periods of the collagen fiber formed. And, from the statistical analyses, we found only insignificant difference (P > 0.05) between the specimens from the various experimental groups. It seems to indicate that the ultimate packing of collagen monomers was probably not interfered or affected significantly by the presence of HA in vitro.

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Section: Resultsmentioning

confidence: 98%

Influences of hyaluronan on type II collagen fibrillogenesis in vitro

Kuo

Wang²,

Niu

et al. 2007

J Mater Sci: Mater Med

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“…32,33 Normally, this collagen is dissolved in an acidic solution (such as acetic acid), and is then reconstituted into fibrils by means of increasing the temperature and/or neutralizing the pH. [13][14][15][16] The ultrastructure of the fibrils depends on the medium conditions, such as pH, temperature, and ionic strength, as well as the sequence of the assembly steps. [13][14][15][16][17] Among the choices in changing the degree of fibril formation, only the incubation period was varied in this study with all the other conditions fixed (pH at ϳ4.2, temperature at 37°C, ionic strength of ϳ123 mM NaCl and the assembly procedure as described in the Method section).…”

Section: Discussionmentioning

confidence: 99%

“…[13][14][15][16] The ultrastructure of the fibrils depends on the medium conditions, such as pH, temperature, and ionic strength, as well as the sequence of the assembly steps. [13][14][15][16][17] Among the choices in changing the degree of fibril formation, only the incubation period was varied in this study with all the other conditions fixed (pH at ϳ4.2, temperature at 37°C, ionic strength of ϳ123 mM NaCl and the assembly procedure as described in the Method section). The lateral interaction between the triple-helical domains basically accounts for the self-assembly process of the collagen.…”

Section: Discussionmentioning

confidence: 99%

“…In addition, there was a significant amount of seemingly unassembled collagen, a state similar to the aggregates found in a collagen-dissolved solution, which is known to consist of ϳ1.5-nm diameter collagen monomers (not clearly revealed in the electron micro- graph). 13 This monomer collagen state constitutes most of the collagen coating without the assembly process. However, with the prolonged assembly for 8 h, almost all the collagen fibrils were in the state of the large-sized mature form.…”

Section: Discussionmentioning

confidence: 99%

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Fibrillar assembly and stability of collagen coating on titanium for improved osteoblast responses

Kim

Lee

et al. 2005

J Biomedical Materials Res

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Collagen, as a major constituent of human connective tissues, has been regarded as one of the most important biomaterials. As a coating moiety on Ti hard-tissue implants, the collagen has recently attracted a great deal of attention. This article reports the effects of fibrillar assembly and crosslinking of collagen on its chemical stability and the subsequent osteoblastic responses. The fibrillar self-assembly of collagen was carried out by incubating acid-dissolved collagen in an ionic-buffered medium at 37 degrees C. The degree of assembly was varied with the incubation time and monitored by the turbidity change. The differently assembled collagen was coated on the Ti and crosslinked with a carbodiimide derivative. The partially assembled collagen contained fibrils with varying diameters as well as nonfibrillar aggregates. On the other hand, the fully assembled collagen showed the complete formation of fibrils with uniform diameters of approximately 100-200 nm with periodic stain patterns within the fibrils, which are typical of native collagen fibers. Through this fibrillar assembly, the collagen coating had significantly improved chemical stability in both the saline and collagenase media. The subsequent crosslinking step also improved the stability of the collagen coating, particularly in the unassembled collagen. The fibrillar assembly and the crosslinking of collagen significantly influenced the osteoblastic cell responses. Without the assembly, the collagen layer on Ti adversely affected the cell attachment and proliferation. However, those cellular responses were improved significantly when the collagen was assembled to fibrils and the assembly degree was increased. After crosslinking the collagen coating, these cellular responses were significantly enhanced in the case of the unassembled collagen but were not altered much in the assembled collagen. Based on these observations, it is suggested that the fibrillar assembly and the crosslinking of collagen require careful considerations in the collagen administration as a coating moiety.

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“…[27,28] Recent work on the abnormal assembly of collagen into FLS collagen has indicated that there may be lateral assembly of 4D-period staggered microfibril subunits. [29] The proposed mechanism for the fibrillogenesis pathway for this FLS collagen has been a stepwise process of initial formation of microfibrils, binding of a1-acid glycoproteins to the collagen, followed by lateral association of the fibrils. [29] The use of soluble type I collagen, without addition of a1-acid glycoproteins in the present study means that we are dealing with native fibrils rather than FLS collagen aggregates.…”

Section: Full Papermentioning

confidence: 99%

Engineering Functional Collagen Scaffolds: Cyclical Loading Increases Material Strength and Fibril Aggregation

Cheema

Chuo

Sarathchandra

et al. 2007

Adv Funct Materials

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Variation in collagen fibril diameter in nature is a major factor determining biological material properties. However, the mechanism resulting in this fibril diameter difference is not clear and generally assumed to be cell‐dependent. It is certainly not possible so far to engineer this into implantable scaffold materials. This gap in our knowledge is crucial for the fabrication of truly biomimetic tissue‐like materials. We have tested the idea that fibril diameter can be regulated directly without cell involvement, using cyclical mechanical loading to promote fibril fusion. Specific loading regimes increased collagen fibril diameter (> 2 fold) in direct relation to cycle number, whilst thin fibrils disappeared. Tensile properties increased, producing a 4.5 fold rise in break strength. This represents the first demonstration of direct cyclical load‐promoted fibril fusion and provides a direct relation with material properties. The ability to control material properties in this way makes it possible to fabricate truly biomimetic collagen materials without cells.

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Hierarchical assembly and the onset of banding in fibrous long spacing collagen revealed by atomic force microscopy

Cited by 31 publications

References 51 publications

Influences of hyaluronan on type II collagen fibrillogenesis in vitro

Influences of hyaluronan on type II collagen fibrillogenesis in vitro

Fibrillar assembly and stability of collagen coating on titanium for improved osteoblast responses

Engineering Functional Collagen Scaffolds: Cyclical Loading Increases Material Strength and Fibril Aggregation

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