2019
DOI: 10.1002/cbic.201900202
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Direct Radiation Effects on the Structure and Stability of Collagen and Other Proteins

Abstract: In this review, recent progress in understanding the direct effects of radiation on the structure and stability of collagen, the most abundant protein in the human body, and other proteins is surveyed. Special emphasis is placed on the triple‐helical structure of collagen, as studied by means of collagen mimetic peptides. The emerging patterns are the dose dependence of radiation processes and their abundance, the crucial role of radicals in covalent‐bond formation (crosslinking) or cleavage, and the influence… Show more

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Cited by 21 publications
(16 citation statements)
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“…Organic solvents or detergents will alter hydrophobic interactions, and stability of enzymes in organic solvents will be dependent on the ability of the solvent to strip the essential hydration layer from the protein surface [25,26]. Last but not least, mechanical stress or radiation may disrupt the delicate balance of forces that maintain protein structure [27]. Stabilizing the enzyme means preventing these changes.…”
Section: Intrinsic (In)stability Of Enzymesmentioning
confidence: 99%
“…Organic solvents or detergents will alter hydrophobic interactions, and stability of enzymes in organic solvents will be dependent on the ability of the solvent to strip the essential hydration layer from the protein surface [25,26]. Last but not least, mechanical stress or radiation may disrupt the delicate balance of forces that maintain protein structure [27]. Stabilizing the enzyme means preventing these changes.…”
Section: Intrinsic (In)stability Of Enzymesmentioning
confidence: 99%
“…In contrast to UVR, photons of ionising radiation are energetic enough to ionise most molecules and atoms [ 92 ], potentially leading to the disruption of intermolecular bonds [ 93 ]. An abundance of water molecules in biological systems results in a large percentage of ionising radiation being absorbed by water in a process called water radiolysis [ 94 ], producing multiple ROS species.…”
Section: Ionising Radiation (X-rays/gamma Rays)mentioning
confidence: 99%
“…UVR can also damage the ECM via acellular pathways. Whilst degradation and breakdown of the triple helical structure of collagen can be mediated by photodynamically produced ROS [ 93 , 105 ], high UVR doses and/or non-environmentally attainable wavelengths are commonly required to induce measurable structural and functional effects on fibrillar collagens [ 124 ]. We have previously shown [ 74 , 76 , 146 ] that ECM proteins that are particularly enriched in UV chromophore amino acid residues are susceptible to UVR-induced degradation compared with UV chromophore-poor proteins such as collagen I and elastin.…”
Section: Model Tissue Systems For Radiation Studiesmentioning
confidence: 99%
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“…Third, the type and strength of ionizing radiation play a crucial role. The plausible mechanisms and molecular outcomes of ionizing radiation on proteins have been thoroughly examined in [18].…”
Section: Introductionmentioning
confidence: 99%