Thermodynamic and structural characteristics of collagen fibrils formed in vitro at different temperatures and concentrations

Nikolaeva, T. I.; Tiktopulo, E. I.; Polozov, R. V.; Rochev, Yury

doi:10.1134/s000635090702008x

Cited by 11 publications

(7 citation statements)

References 29 publications

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“…It is known that fibril diameter varies widely with temperature, water content and collagen tissue [18] , [29] – [31] . The physical or developmental reasons for a large variation among tissues remain poorly understood.…”

Section: Materials and Experimental Methodsmentioning

confidence: 99%

“…Water is generally expected to be highly relevant for the physics of biopolymers [14] – [17] , and collagen is not an exclusion in this respect [3] , [18] – [22] . This requires understanding of two different influences: that of the solvent water on the polymer structure and the inverse influence of the polymer on the ambient water [15] .…”

Section: Introductionmentioning

confidence: 99%

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Stabilization and Anomalous Hydration of Collagen Fibril under Heating

et al. 2013

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BackgroundType I collagen is the most common protein among higher vertebrates. It forms the basis of fibrous connective tissues (tendon, chord, skin, bones) and ensures mechanical stability and strength of these tissues. It is known, however, that separate triple-helical collagen macromolecules are unstable at physiological temperatures. We want to understand the mechanism of collagen stability at the intermolecular level. To this end, we study the collagen fibril, an intermediate level in the collagen hierarchy between triple-helical macromolecule and tendon.Methodology/Principal FindingWhen heating a native fibril sample, its Young’s modulus decreases in temperature range 20–58°C due to partial denaturation of triple-helices, but it is approximately constant at 58–75°C, because of stabilization by inter-molecular interactions. The stabilization temperature range 58–75°C has two further important features: here the fibril absorbs water under heating and the internal friction displays a peak. We relate these experimental findings to restructuring of collagen triple-helices in fibril. A theoretical description of the experimental results is provided via a generalization of the standard Zimm-Bragg model for the helix-coil transition. It takes into account intermolecular interactions of collagen triple-helices in fibril and describes water adsorption via the Langmuir mechanism.Conclusion/SignificanceWe uncovered an inter-molecular mechanism that stabilizes the fibril made of unstable collagen macromolecules. This mechanism can be relevant for explaining stability of collagen.

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Section: Materials and Experimental Methodsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Stabilization and Anomalous Hydration of Collagen Fibril under Heating

et al. 2013

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“…The experimental variables applied in vitro will influence the kinetics of collagen self-assembly and its morphology, such as concentration, pH and ionic strength (Nikolaeva, Tiktopulo, Polozov, & Rochev, 2007;Noitup et al, 2006;Sang et al, 2010). The kinetics research of collagen assembly can display the selfassembly mechanism and give methods to control the assembly process (Shui & Zhou, 2005).…”

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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“…Type I COLL is an appealing candidate for CNS applications because of its ability to self-assemble and form a fibrillar structure in physiological conditions without a crosslinking agent, thus reducing the risk of inflammation and cytotoxicity at the injection site. We selected a final COLL concentration of 1.2 mg/mL, because under physiological conditions (35-37°C, pH 7.2), COLL fibrils are formed more rapidly at this concentration and the enthalpy of their assembly is minimal 15 . HA is a major extracellular matrix component in the brain, is involved in the development and homeostasis of the CNS, and its biological functions depend on the molecular weight 16,17 .…”

Section: Introductionmentioning

confidence: 99%

“…a After electrophoretic separation on 8% gradient polyacrylamide gels, we performed silver staining on the supernatants collected from Tat-Hsp70-loaded composites (4 replicates: 1, 2, 3, 4) in PBS after 1, 4, 24, 72, 96, and 168 h (7 days). For each gel, we used five standards (s1 = 0.15 µg; s2 = 0.2 µg; s3 = 0.25 µg; s4 = 0.3 µg; s5 = 0.35 µg) and loaded35,19,12,10,15, 55, and 55 µL supernatants collected after 1, 4, 24, 72 (A), 72 (B), 96, and 168 h, respectively. b Example of a calibration line used to estimate the amount of Tat-Hsp70 from the optical density of the bands visualized by silver staining.…”

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confidence: 99%

Hydrogel-based delivery of Tat-fused protein Hsp70 protects dopaminergic cells in vitro and in a mouse model of Parkinson’s disease

et al. 2019

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Neurodegenerative disorders such as Parkinson's disease (PD) have no effective therapies. However, many promising drugs are precluded from clinical trials because of their poor brain availability. The chaperone protein Hsp70 has been reported to be effective in PD models, but its brain targeting is challenging. We developed a novel brain Hsp70 delivery system using injectable, biocompatible, and biodegradable semi-interpenetrating polymer networks of collagen (COLL) and low-molecular-weight hyaluronic acid (LMW HA) structured with gelatin particles. We produced human recombinant Hsp70-1A fused with the cell-penetrating peptide Tat (Tat-Hsp70) that was neuroprotective in vitro against the dopaminergic toxin 6-hydroxydopamine (6-OHDA). We assessed Tat-Hsp70 release from the selected COLL-LMW HA composites in vitro, observing a 95% release of loaded protein after 96 h. The release kinetics FITTED the Korsmeyer-Peppas model (regression coefficient 0.98) and the released Tat-Hsp70 remained neuroprotective for SH-SY5Y cells. Magnetic resonance imaging revealed that COLL-LMW HA composites lasted at least 96 h at the brain level, and in vivo Tat-Hsp70 release studies indicated that hydrogel presence is pivotal for a spatially focused neuroprotective effect. In an in vivo model of dopaminergic degeneration, Tat-Hsp70-loaded composites conveyed neuroprotection at both the behavioral and dopaminergic neuronal levels against the striatal injection of 6-OHDA. After the injection of Tat-Hsp70-loaded composites, mice showed a transient inflammatory response, with a decrease in GFAP and CD11b immunostaining after 7 days. Our delivery system enabled the effective brain release of Tat-Hsp70 and is ready for further improvements.

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Thermodynamic and structural characteristics of collagen fibrils formed in vitro at different temperatures and concentrations

Cited by 11 publications

References 29 publications

Stabilization and Anomalous Hydration of Collagen Fibril under Heating

Stabilization and Anomalous Hydration of Collagen Fibril under Heating

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

Hydrogel-based delivery of Tat-fused protein Hsp70 protects dopaminergic cells in vitro and in a mouse model of Parkinson’s disease

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