High pressure stabilization of collagen structure

Potekhin, Sergey A.; Senin, Alexander A.; Abdurakhmanov, N.N.; Tiktopulo, E. I.

doi:10.1016/j.bbapap.2009.04.005

Cited by 42 publications

(22 citation statements)

References 91 publications

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“…An earlier study of acid soluble collagen extracted from the skin of a 3-month-old pig, in which collagen is not highly cross-linked, suggested that pressure values higher than 0.32 GPa destabilize the collagen structure [56]. However, our study clearly demonstrates much higher pressure range stability for collagen extracted from bovine Achilles tendon.…”

Section: Discussioncontrasting

confidence: 49%

High pressure Raman study of type‐I collagen

et al. 2018

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The high pressure response of type-I collagen from bovine Achilles tendon is investigated with micro-Raman spectroscopy. Fluorinert™ and methanol-ethanol mixtures were used as pressure transmitting media (PTM) in a diamond anvil cell. The Raman spectrum of collagen is dominated by three bands centred at approximately 1450, 1660 and 2930 cm , attributed to C-H deformation, C=O stretching of the peptide bond (amide-I band) and C-H stretching modes respectively. Upon pressure increase, using Fluorinert™ as PTM, a shift towards higher frequencies of the C-H stretching and deformation peaks is observed. Contrary, the amide-I band peaks are shifted to lower frequencies with moderate pressure slopes. On the other hand, when using the alcohol mixture as PTM, the amide-I band exhibits more pronounced C=O bond softening, deduced from the shift to lower frequencies, suggesting a strengthening of the hydrogen bonds between glycine and proline residues of different collagen chains due to the presence of the polar alcohol molecules. Furthermore, some of the peaks exhibit abrupt changes in their pressure slopes at approximately 2 GPa, implying a variation in the compressibility of the collagen fibres. This could be attributed to a pitch change from 10/3 to 7/2, sliding of the tropocollagen molecules, twisting variation at the molecular level and/or elimination of the D-gaps induced by kink compression. All spectral changes are reversible upon pressure release, which indicates that denaturation has not taken place. Finally, a minor lipid phase contamination was detected in some sample spots. Its pressure response is also monitored.

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Section: Discussioncontrasting

confidence: 49%

High pressure Raman study of type‐I collagen

et al. 2018

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“…Water is the universal and natural solvent for proteins, dictating the molecular motions, the structure and function of these molecules [22]. Globular proteins are only marginally stable, and such metastability makes proteins difficult to handle experimentally [12,13,18,[50][51][52][53]. According to Bizzarri and Cannistraro [54], a threshold level of hydration (0.4 g water /g protein ) is required to fully activate the functionality of globular proteins, an amount less than would be necessary for a complete coverage of the surface of the protein.…”

Section: Introductionmentioning

confidence: 99%

Structural and functional stabilization of protein entities: state-of-the-art

Balcão

Vila

2015

Advanced Drug Delivery Reviews

199

104

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Within the context of biomedicine and pharmaceutical sciences, the issue of (therapeutic) protein stabilization assumes particular relevance. Stabilization of protein and protein-like molecules translates into preservation of both structure and functionality during storage and/or targeting, and such stabilization is mostly attained through establishment of a thermodynamic equilibrium with the (micro)environment. The basic thermodynamic principles that govern protein structural transitions and the interactions of the protein molecule with its (micro)environment are, therefore, tackled in a systematic fashion. Highlights are given to the major classes of (bio)therapeutic molecules, viz. enzymes, recombinant proteins, (macro)peptides, (monoclonal) antibodies and bacteriophages. Modification of the microenvironment of the biomolecule via multipoint covalent attachment onto a solid surface followed by hydrophilic polymer co-immobilization, or physical containment within nanocarriers, are some of the (latest) strategies discussed aiming at full structural and functional stabilization of said biomolecules.

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“…This could be due to the influence of ultrahigh pressure on hydrogen bonds. It has been reported that UHP can disturb the balance of hydrogen bonds in collagen (Potekhin et al ., ). However, the frequencies of amide A were not clearly changed with an increase in the acid concentration, which implies that some of the hydrogen bonds could be mainly influenced by UHP and then the covalent bonds could be mainly damaged by the acid concentration used in this process.…”

Section: Resultsmentioning

confidence: 97%

Effects of acid concentration and the UHP pretreatment on the gelatinisation of collagen and the properties of extracted gelatins

Zhang

Cai

et al. 2016

Int J of Food Sci Tech

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An ultra-high-pressure (UHP) transmission medium with HCl was applied as a pretreatment to extract gelatin. The effects of the acid concentration (0-1% (w/v)) on the gelatinisation of collagen and the properties of gelatin were investigated. An increase in the acid concentration decreased the thermostability of collagen and increased the yield of gelatin (from 64% increased to 80%). The content of the subunit components in the pretreated collagen and the gelatin declined slightly as the acid concentration was increased, resulted in slight decrease (P > 0.05) in the gel strength (from 435 g decreased to 408 g). The analysis of Fourier transform infrared spectroscopy (FTIR) spectra showed that the triple-helical structure, secondary structures of the collagen and covalent cross-linking in the collagenous fibres were damaged gradually as the acid concentration was increased. The scanning electron microscopy (SEM) images showed that the smooth surface of collagen was partly disrupted with microvoids after UHP/1% HCl pretreatment, which may be related to the damage on the covalent cross-linking.

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High pressure stabilization of collagen structure

Cited by 42 publications

References 91 publications

High pressure Raman study of type‐I collagen

High pressure Raman study of type‐I collagen

Structural and functional stabilization of protein entities: state-of-the-art

Effects of acid concentration and the UHP pretreatment on the gelatinisation of collagen and the properties of extracted gelatins

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