Formaldehyde-mediated aggregation of protein antigens: Comparison of untreated and formalinized model antigens

Jiang, Wenlei; Schwendeman, Steven P.

doi:10.1002/1097-0290(20001205)70:5<507::aid-bit5>3.0.co;2-c

Cited by 38 publications

(40 citation statements)

References 28 publications

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“…Furthermore, RNase A is a single chain polypeptide containing 4 disulfide bridges [44]. Previous gel electrophoresis study has showed that formaldehyde treatment of RNase A leads to a rapid formation of protein cross-links [45], [46]. Thus, RNase A was used as a positive control in our experiments.…”

Section: Discussionmentioning

confidence: 99%

Formaldehyde at Low Concentration Induces Protein Tau into Globular Amyloid-Like Aggregates In Vitro and In Vivo

et al. 2007

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Recent studies have shown that neurodegeneration is closely related to misfolding and aggregation of neuronal tau. Our previous results show that neuronal tau aggregates in formaldehyde solution and that aggregated tau induces apoptosis of SH-SY5Y and hippocampal cells. In the present study, based on atomic force microscopy (AFM) observation, we have found that formaldehyde at low concentrations induces tau polymerization whilst acetaldehyde does not. Neuronal tau misfolds and aggregates into globular-like polymers in 0.01–0.1% formaldehyde solutions. Apart from globular-like aggregation, no fibril-like polymerization was observed when the protein was incubated with formaldehyde for 15 days. SDS-PAGE results also exhibit tau polymerizing in the presence of formaldehyde. Under the same experimental conditions, polymerization of bovine serum albumin (BSA) or α-synuclein was not markedly detected. Kinetic study shows that tau significantly misfolds and polymerizes in 60 minutes in 0.1% formaldehyde solution. However, presence of 10% methanol prevents protein tau from polymerization. This suggests that formaldehyde polymerization is involved in tau aggregation. Such aggregation process is probably linked to the tau's special “worm-like” structure, which leaves the ε-amino groups of Lys and thiol groups of Cys exposed to the exterior. Such a structure can easily bond to formaldehyde molecules in vitro and in vivo. Polymerizing of formaldehyde itself results in aggregation of protein tau. Immunocytochemistry and thioflavin S staining of both endogenous and exogenous tau in the presence of formaldehyde at low concentrations in the cell culture have shown that formaldehyde can induce tau into amyloid-like aggregates in vivo during apoptosis. The significant protein tau aggregation induced by formaldehyde and the severe toxicity of the aggregated tau to neural cells may suggest that toxicity of methanol and formaldehyde ingestion is related to tau misfolding and aggregation.

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Section: Discussionmentioning

confidence: 99%

Formaldehyde at Low Concentration Induces Protein Tau into Globular Amyloid-Like Aggregates In Vitro and In Vivo

et al. 2007

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“…35 Although peptide cleavage rates have not been directly related to PLGA hydrolysis rates, the hydrolysis of Asp-Pro bonds in bovine serum albumin (BSA) was prevented by switching from a 50/50 PLGA to PLA-PEG. 44 Because hydrolysis of the BSA AspPro bond is acid catalyzed, 45 degradation of this protein was mediated by encapsulation in polymer system that did not allow for the accumulation of acidic monomers and oligomers.…”

Section: Amide Bond Hydrolysismentioning

confidence: 99%

Chemical Degradation of Peptides and Proteins in PLGA: A Review of Reactions and Mechanisms

Houchin

Topp

2008

Journal of Pharmaceutical Sciences

244

155

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“…The main reason may be that the NH or NH 2 groups in L-histidine molecule can react with formaldehyde, 33,34 and their reaction is described by equation (10).…”

Section: Mechanism Of Formaldehyde Releasementioning

confidence: 99%

Release behavior and kinetic evaluation of formaldehyde from cotton clothing fabrics finished with DMDHEU-based durable press agents in water and synthetic sweat solution

Dong

Wang

et al. 2016

Textile Research Journal

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The durable press-finished cotton fabrics were prepared with dimethylol dihydroxy ethylene urea (DMDHEU) and methylated DMDHEU, and tested for formaldehyde release in distilled water or synthetic sweat at pH 5 or 8 to simulate the extraction of formaldehyde by sweat under similar wearing conditions. The release mechanism of formaldehyde was studied and compared using three diffusion kinetic models. The effect of release conditions and finishing process on the formaldehyde release was also investigated. The results indicated that the release process of formaldehyde from the finished fabric includes a burst release phase and a slow release phase, which is explained by five different sources. The formaldehyde release mechanism followed the Fickian mode, and could be described by Higuchi, Double phases and Korsmeyer-Peppas kinetic equations, respectively. Higher formaldehyde release was found at pH 8 than that at pH 5. Formaldehyde showed a lower release rate in synthetic sweat solution than that in water under the same conditions. Increasing water volume or temperature enhanced the formaldehyde release, suggesting that a high sweat rate and skin temperature may accelerate the formaldehyde release. When finishing the fabrics, a higher concentration of finishing agent and the addition of softener accelerated the formaldehyde release. However, increasing catalyst concentration and curing temperature could reduce the formaldehyde release. It is concluded that formaldehyde release can be effectively reduced by optimizing the durable press finishing process of cotton fabrics, thus possibly decreasing risk of allergic contact dermatitis from formaldehyde in textiles.Keywords durable press finishing, formaldehyde release, dimethylol dihydroxy ethylene urea, kinetic model Durable press agents (DP agents) are generally used to improve the wrinkle resistance of various clothing fabrics during wear and laundering. However, the majority of DP agents often contain significant levels of formaldehyde because they are created from the condensation product of formaldehyde with urea or melamine. Formaldehyde is a known human carcinogen, 1,2 which is released from the cotton clothing fabrics finished with formaldehyde-based DP agents in the last decades. Previous study 3 has found that large amounts of formaldehyde were concentrated in skin next to the durable press garment and relatively small amounts enter the body when rabbits were used as the test subjects. In the 1950s and 1960s, allergic contact

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Formaldehyde-mediated aggregation of protein antigens: Comparison of untreated and formalinized model antigens

Cited by 38 publications

References 28 publications

Formaldehyde at Low Concentration Induces Protein Tau into Globular Amyloid-Like Aggregates In Vitro and In Vivo

Formaldehyde at Low Concentration Induces Protein Tau into Globular Amyloid-Like Aggregates In Vitro and In Vivo

Chemical Degradation of Peptides and Proteins in PLGA: A Review of Reactions and Mechanisms

Release behavior and kinetic evaluation of formaldehyde from cotton clothing fabrics finished with DMDHEU-based durable press agents in water and synthetic sweat solution

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