UV Light Effects on Proteins: From Photochemistry to Nanomedicine

Neves‐Petersen, Maria Teresa; Gajula, Gnana Prakash; Petersen, Steffen B.

doi:10.5772/37947

Cited by 23 publications

(12 citation statements)

References 103 publications

(70 reference statements)

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“…Phe can dissociate to form a highly reactive benzyl radical, and is most relevant, since Tyr and Trp, although absorbing more strongly, occur far less frequently in the helical domains of the fibrillar collagens. It would be of concern if the phenylalanine side chain in the GFOGER motif was involved in such photoreactions [54] , as integrin-reactivity would be compromised directly. Indeed, increasing covalent linkage between collagen and ES-GFOGER could be observed after extended exposure, despite using much longer wavelength, 365 nm, than the 200–254 nm absorption peak of the aromatic sidechains described above.…”

Section: Discussionmentioning

confidence: 99%

The synthesis and coupling of photoreactive collagen-based peptides to restore integrin reactivity to an inert substrate, chemically-crosslinked collagen

et al. 2016

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Collagen is frequently advocated as a scaffold for use in regenerative medicine. Increasing the mechanical stability of a collagen scaffold is widely achieved by cross-linking using 1-ethyl-3-(3-dimethylaminopropyl)carbodiimide (EDC) and N-hydroxysuccinimide (NHS). However, this treatment consumes the carboxylate-containing amino acid sidechains that are crucial for recognition by the cell-surface integrins, abolishing cell adhesion. Here, we restore cell reactivity to a cross-linked type I collagen film by covalently linking synthetic triple-helical peptides (THPs), mimicking the structure of collagen. These THPs are ligands containing an active cell-recognition motif, GFOGER, a high-affinity binding site for the collagen-binding integrins. We end-stapled peptide strands containing GFOGER by coupling a short diglutamate-containing peptide to their N-terminus, improving the thermal stability of the resulting THP. A photoreactive Diazirine group was grafted onto the end-stapled THP to allow covalent linkage to the collagen film upon UV activation. Such GFOGER-derivatized collagen films showed restored affinity for the ligand-binding I domain of integrin α2β1, and increased integrin-dependent cell attachment and spreading of HT1080 and Rugli cell lines, expressing integrins α2β1 and α1β1, respectively. The method we describe has wide application, beyond collagen films or scaffolds, since the photoreactive diazirine will react with many organic carbon skeletons.

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Section: Discussionmentioning

confidence: 99%

The synthesis and coupling of photoreactive collagen-based peptides to restore integrin reactivity to an inert substrate, chemically-crosslinked collagen

et al. 2016

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“…The radical electron is carried on, potentially attacking new molecules in a chain reaction. It has been suggested that a radical moiety can travel along a protein backbone , until it finds a suitable reaction site or is trapped by a disulfide bridge and finally lost. When analyzing proteins, peptides and amino acids we detect a substantial proportion of oxidized analyte after it passed the UV flow cell.…”

Section: Resultsmentioning

confidence: 99%

HPLC–UV–MS Analysis: A Source for Severe Oxidation Artifacts

Schweikart

Hulthe

2019

Anal. Chem.

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HPLC coupled to both UV and MS is an established setup for purity assessments in many areas. With evolving technology, instrument sensitivity increases, calling for lower sample concentration, while light flux in a commercial UV detector cell is considerably higher than earlier. This evolution has now reached the point where radicals formed by UV light are abundant enough, compared to the analyte levels, to generate unwanted artifact signals in the MS spectrum. In this work we show several examples from pharmaceutical development where UV degradation in the UV detector leads to severely misleading mass spectra in typical day to day samples.

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“…The electron can then be captured by disulfide bridges, leading to their dissociation. 47 This disulfide bond dissociation can result in conformational changes of the protein. The extent of UV−C-induced conformational changes in proteins depends on various factors, including the specific amino acid composition, protein structure, UV−C dosage, exposure time, and environmental conditions.…”

Section: ■ Discussionmentioning

confidence: 99%

Optimized Ultraviolet-C Processing Inactivates Pathogenic and Spoilage-Associated Bacteria while Preserving Bioactive Proteins, Vitamins, and Lipids in Human Milk

Liang,

Mohamed,

Pung

et al. 2024

J. Agric. Food Chem.

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Holder pasteurization (HoP) enhances donor human milk microbiological safety but damages many bioactive milk proteins. Though ultraviolet-C irradiation (UV−C) can enhance safety while better preserving some milk proteins, it has not been optimized for dose or effect on a larger array of bioactive proteins. We determined the minimal UV−C parameters that provide >5log reductions of relevant bacteria in human milk and how these treatments affect an array of bioactive proteins, vitamin E, and lipid oxidation. Treatment at 6000 and 12 000 J/L of UV−C resulted in >5-log reductions of all vegetative bacteria and bacterial spores, respectively. Both dosages improved retention of immunoglobulin A (IgA), IgG, IgM, lactoferrin, cathepsin D, and elastase and activities of bile-salt-stimulated lipase and lysozyme compared with HoP. These UV−C doses caused minor reductions in αtocopherol but not γ-tocopherol and no increases in lipid oxidation products. UV−C treatment is a promising approach for donor human milk processing.

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UV Light Effects on Proteins: From Photochemistry to Nanomedicine

Cited by 23 publications

References 103 publications

The synthesis and coupling of photoreactive collagen-based peptides to restore integrin reactivity to an inert substrate, chemically-crosslinked collagen

The synthesis and coupling of photoreactive collagen-based peptides to restore integrin reactivity to an inert substrate, chemically-crosslinked collagen

HPLC–UV–MS Analysis: A Source for Severe Oxidation Artifacts

Optimized Ultraviolet-C Processing Inactivates Pathogenic and Spoilage-Associated Bacteria while Preserving Bioactive Proteins, Vitamins, and Lipids in Human Milk

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