Collagen entanglement influenced by the addition of acids

Oechsle, Anja Maria; Wittmann, Xandra; Gibis, Monika; Kohlus, Reinhard; Weiß, Jochen

doi:10.1016/j.eurpolymj.2014.06.015

Cited by 41 publications

(24 citation statements)

References 41 publications

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“…3). The significant reduction in G 0 is also consistent with findings from lower-frequency bulk rheology (31).…”

Section: Effects Of Telopeptides On Viscoelastic Propertiessupporting

confidence: 80%

“…3 shows measured elastic and viscous moduli, G 0 (f) and G 00 (f), determined for commercially obtained telo-and atelo-collagen molecules in acidic solution at nominal concentrations of 2 mg/ml. This concentration lies above the estimated overlap concentration of c* z 1 mg/ml (22,31). A clear feature is the significantly higher elastic moduli of the telo-collagen solution below 300 Hz.…”

Section: Effects Of Telopeptides On Viscoelastic Propertiesmentioning

confidence: 67%

“…is modeled as a Rouse chain, with intramolecular relaxation timescales as given in (27). At higher concentrations where the solution is no longer in the dilute limit (c* for collagen in acidic conditions has been estimated at 1 mg/ml (22,31)), transverse relaxation of slower, longer-range modes is constrained. From the spectrum of (partially constrained) Rouse modes for each species, a stress-relaxation modulus is calculated; the contribution of the modulus of each species to the overall relaxation modulus of the system is then weighted by its number concentration in solution (Eq.…”

Section: Collagen Modeled As Multimeric Polymer Assemblies In Chemicamentioning

confidence: 99%

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Intact Telopeptides Enhance Interactions between Collagens

Shayegan

Altindal

Kiefl

et al. 2016

Biophysical Journal

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Collagen is the fundamental structural component of a wide range of connective tissues and of the extracellular matrix. It undergoes self-assembly from individual triple-helical proteins into well-ordered fibrils, a process that is key to tissue development and homeostasis, and to processes such as wound healing. Nucleation of this assembly is known to be slowed considerably by pepsin removal of short nonhelical regions that flank collagen's triple helix, known as telopeptides. Using optical tweezers to perform microrheology measurements, we explored the changes in viscoelasticity of solutions of collagen with and without intact telopeptides. Our experiments reveal that intact telopeptides contribute a significant frequency-dependent enhancement of the complex shear modulus. An analytical model of polymers associating to establish chemical equilibrium among higher-order species shows trends in G 0 and G 00 consistent with our experimental observations, including a concentration-dependent crossover in G 00 /c around 300 Hz. This work suggests that telopeptides facilitate transient intermolecular interactions between collagen proteins, even in the acidic conditions used here.

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“…3). The significant reduction in G 0 is also consistent with findings from lower-frequency bulk rheology (31).…”

Section: Effects Of Telopeptides On Viscoelastic Propertiessupporting

confidence: 80%

Section: Effects Of Telopeptides On Viscoelastic Propertiesmentioning

confidence: 67%

Section: Collagen Modeled As Multimeric Polymer Assemblies In Chemicamentioning

confidence: 99%

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Intact Telopeptides Enhance Interactions between Collagens

Shayegan

Altindal

Kiefl

et al. 2016

Biophysical Journal

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“…For telopeptide-poor collagen the protein concentration of the gel was determined in a former study (Oechsle et al, 2014). For the other proteins this information was deduced from the technical data sheet.…”

Section: Sample Preparationmentioning

confidence: 99%

“…In addition to the impact of various acids and pH values, as studied by Oechsle et al (Oechsle, Wittmann, Gibis, Kohlus, & Weiss, 2014), co-gelling proteins affect collagen gel properties that might improve the film quality of the co-extruded collagen casings. In this study, food grade proteins, namely whey protein isolate, blood plasma protein, soy protein isolate, and gluten, were incorporated into the collagen gel matrix to modify microstructure and rheology.…”

Section: Introductionmentioning

confidence: 99%

Modulation of the rheological properties and microstructure of collagen by addition of co-gelling proteins

et al. 2015

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Effect of in situ apatite on performance of collagen fiber film for food packaging applications

Wang

Liu

et al. 2016

J of Applied Polymer Sci

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This study attempted to prepare apatite in situ in acid‐swollen cowhide collagen film by an ammonia gas fumigating method and assess its reinforcement effect on a collagen fiber film for food packaging applications. The X‐ray diffraction and Fourier transform infrared spectroscopy results confirmed the successful synthesis of apatite in collagen fiber films. SEM images showed that tiny apatite particles appeared as a coating on the film surface and also made the film's inner structure more compact and less porous than pure collagen fiber film. Apatite significantly (p < 0.05) increased the tensile strength and improved the water vapor barrier and water insolubility properties of collagen fiber film. Moreover, the thermogravimetric and differential scanning calorimetry results confirmed that the thermal stability of collagen was improved with the increasing apatite. The in situ–synthesized apatite provided a practical reinforcement approach to improving the collagen fiber film's performance and benefited its application as a food packaging material. © 2016 Wiley Periodicals, Inc. J. Appl. Polym. Sci. 2016, 133, 44154.

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Collagen entanglement influenced by the addition of acids

Cited by 41 publications

References 41 publications

Intact Telopeptides Enhance Interactions between Collagens

Intact Telopeptides Enhance Interactions between Collagens

Modulation of the rheological properties and microstructure of collagen by addition of co-gelling proteins

Effect of in situ apatite on performance of collagen fiber film for food packaging applications

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