Nanoscale measurements of the assembly of collagen to fibrils

Yadavalli, Vamsi K.; Svintradze, David V.; Pidaparti, Ramana M.

doi:10.1016/j.ijbiomac.2010.02.012

Cited by 47 publications

(39 citation statements)

References 44 publications

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“…Studies show that collagen is able to self-assemble at 25e37 C and near neutral pH in vitro (Huelin, Baker, Poduska, & Merschrod, 2007;Na, Butz, Bailey, & Carroll, 1986). It can be fabricated into various forms by varying the aggregation conditions, such as fibril, gel, and sponge (Jackson & Fessler, 1955;Swatschek, Schatton, Kellermann, Müller, & Kreuter, 2002;Yadavalli, Svintradze, & Pidaparti, 2010), widely applied in food, cosmetic, and biomedical materials, and tissue engineering. Besides, the physicochemical properties of collagen are influenced by its assembly state (Usha, Jaimohan, Rajaram, & Mandal, 2010;Yang, Wang, Regenstein, & Rouse, 2007).…”

Section: Introductionmentioning

confidence: 99%

Effect of concentration, pH and ionic strength on the kinetic self-assembly of acid-soluble collagen from walleye pollock (Theragra chalcogramma) skin

Yan

Zhao

et al. 2012

Food Hydrocolloids

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Section: Introductionmentioning

confidence: 99%

Effect of concentration, pH and ionic strength on the kinetic self-assembly of acid-soluble collagen from walleye pollock (Theragra chalcogramma) skin

Yan

Zhao

et al. 2012

Food Hydrocolloids

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“…To get insight into the molecular mechanisms of collagen assembly, transmission electron microscopy (TEM) is routinely used at different stages to obtain highly resolved images at the nanometer scale [8]. The structure of collagen fibrils and the kinetics of fibrillogenesis have also been investigated using atomic force microscopy [9,10] which enables in situ imaging in liquid solutions. However, there is a need for non-invasive 3D imaging techniques to monitor and quantify collagen assembly in a 3D environment.…”

Section: Introductionmentioning

confidence: 99%

In situ three-dimensional monitoring of collagen fibrillogenesis using SHG microscopy

Bancelin¹,

Aimé²,

Coradin³

et al. 2012

Biomed. Opt. Express

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We implemented in situ time-lapse Second Harmonic Generation (SHG) microscopy to monitor the three-dimensional (3D) self-assembly of collagen in solution. As a proof of concept, we tuned the kinetics of fibril formation by varying the pH and measured the subsequent exponential increase of fibril volume density in SHG images. We obtained significantly different time constants at pH = 6.5 ± 0.3 and at pH = 7.5 ± 0.3. Moreover, we showed that we could focus on the growth of a single isolated collagen fibril because SHG microscopy is sensitive to well-organized fibrils with diameter below the optical resolution. This work illustrates the potential of SHG microscopy for the rational design and characterization of collagen-based biomaterials.

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“…Many of the physical interactions between ECs and macromolecular components of the ECM, including collagens and fibronectin (Fn), occur at the micron and submicron scale. As the most abundant ECM component, collagen monomers are within the nanoscale regime, approximately 300 nm in width and 1.5 nm in diameter 4, 5. When forming self‐assembled fibrillar structures, collagen molecules extend several micrometers in length and hundreds of nanometers in diameter 6.…”

Section: Introductionmentioning

confidence: 99%

Thermal, crystalline, and mechanical properties of octa(3‐chloropropylsilsesquioxane)/ poly(L‐lactic acid) hybrid films

Zhang

Sun

Fang

et al. 2011

J of Applied Polymer Sci

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A series of organic-inorganic hybrid films were prepared based on octa(3-chloropropylsilsesquioxane) (OCPS) and poly(L-lactic acid) (PLLA) via simply solution blending method. The thermal, crystalline and mechanical properties of OCPS/PLLA hybrid films were characterized by Fourier transform infrared, scanning electron microscopy, energy dispersive spectrometer, differential scanning calorimetry (DSC), X-ray diffraction, polarized optical microscopy, thermogravimetric analysis (TGA), and tensile tests. The results showed that OCPS could be dispersed well at molecular level when its content was less than 3 wt % and began to crystallize in PLLA matrix when the content increased to 5 wt %. DSC study revealed that OCPS acted as a plasticizer to decrease both T g and T m of the PLLA matrix at various heating rates. The addition of OCPS did not change the crystal form of PLLA, while had an great influence on the cold crystallization and melting behaviors of PLLA in the second heating cycles. Moreover, the initial crystallinity of OCPS/PLLA was higher than that of pure PLLA. The results suggested that OCPS could be an effective heterogeneous nucleating reagent to promote the crystallization of PLLA. TGA showed that the PLLA thermal degradation mechanism remained unchanged, whereas the weight loss temperatures and residual weights were improved. Tensile tests indicated that the incorporation of OCPS into PLLA matrix changed the tensile behavior of the hybrid films from brittle to ductile, and the strain at break was improved remarkably as a result of the plasticizer effect of OCPS.

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Nanoscale measurements of the assembly of collagen to fibrils

Cited by 47 publications

References 44 publications

Effect of concentration, pH and ionic strength on the kinetic self-assembly of acid-soluble collagen from walleye pollock (Theragra chalcogramma) skin

Effect of concentration, pH and ionic strength on the kinetic self-assembly of acid-soluble collagen from walleye pollock (Theragra chalcogramma) skin

In situ three-dimensional monitoring of collagen fibrillogenesis using SHG microscopy

Thermal, crystalline, and mechanical properties of octa(3‐chloropropylsilsesquioxane)/ poly(L‐lactic acid) hybrid films

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