Use of Raman spectroscopy for the identification of radical-mediated damages in human serum albumin

Jurasekova, Z.; Tinti, Anna; Torreggiani, Armida

doi:10.1007/s00216-011-4970-y

Cited by 26 publications

(18 citation statements)

References 58 publications

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“…The localization of this band below 500 cm −1 indicates that some of these conformers are now found in a restricted medium, the S–S bonds being less flexible [33]. Such bands have been previously reported at 489 [34] and 463 cm −1 [35]. Thus, the ggt conformation of the disulfide bridges is converted to a ggg conformation as a result of protein corona forming onto AuNPs.…”

Section: Resultsmentioning

confidence: 63%

Formation and Stabilization of Gold Nanoparticles in Bovine Serum Albumin Solution

et al. 2019

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The formation and growth of gold nanoparticles (AuNPs) were investigated in pH 7 buffer solution of bovine serum albumin (BSA) at room temperature. The processes were monitored by UV-Vis, circular dichroism, Raman and electron paramagnetic resonance (EPR) spectroscopies. TEM microscopy and dynamic light scattering (DLS) measurements were used to evidence changes in particle size during nanoparticle formation and growth. The formation of AuNPs at pH 7 in the absence of BSA was not observed, which proves that the albumin is involved in the first step of Au(III) reduction. Changes in the EPR spectral features of two spin probes, CAT16 and DIS3, with affinity for BSA and AuNPs, respectively, allowed us to monitor the particle growth and to demonstrate the protective role of BSA for AuNPs. The size of AuNPs formed in BSA solution increases slowly with time, resulting in nanoparticles of different morphologies, as revealed by TEM. Raman spectra of BSA indicate the interaction of albumin with AuNPs through sulfur-containing amino acid residues. This study shows that albumins act as both reducing agents and protective corona of AuNPs.

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Section: Resultsmentioning

confidence: 63%

Formation and Stabilization of Gold Nanoparticles in Bovine Serum Albumin Solution

et al. 2019

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“…This condition has been used as model of oxidative damages occurring in vivo [13][14][15] where • OH radicals play a prominent role.…”

Section: Methodsmentioning

confidence: 99%

Spectroscopic investigation on the structural modifications induced by radical stress on oligopeptides for tissue engineering

Foggia

Torreggiani

Taddei

et al. 2013

J Raman Spectroscopy

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EAK16 (AEAEAKAKAEAEAKAK) and seven alternating polar/hydrophobic oligopeptides (derived from EAK16 by primary structure modifications) were tested for their resistance to free radical attack, in view of their possible use as biomimetic coatings of biomedical devices; in fact, oxidative radical stress, mainly due to hydroxyl radicals (•OH), is a common physiological condition occurring under acute or chronic inflammatory response. •OH radicals, mimicking an endogenous radical stress, were generated by gamma‐radiolysis of water solutions. IR and Raman spectroscopies were used to investigate the damages induced by free radicals on the oligopeptides, in particular on their folding and inter‐chain interactions. Some oligopeptides, i.e. EAK16 (pept1), pept3 (obtained by K → O substitution), pept5 (A → Abu substitution), pept7 (insertion at the N‐terminus of the RGD sequence), and pept8 (RGD insertion and “scrambling” of the sequence) were not severely affected by the treatment and retained their prevalent structure (i.e. α‐helix for pept8 and β‐sheet for the others). The other peptides, i.e. pept2 (obtained by E → D substitution), pept4 (E → D and K → O substitutions) and pept6 (A → Y substitution), showed significant conformational changes (i.e. increase in the α‐helix content) upon irradiation. In pept2 and pept4, modifications in hydrophobic and ionic interactions were observed; the latter were mainly ascribed to the decarboxylation of acidic amino acids. In pept6, the main target of the •OH attack was Tyr, as deduced by the strong variations observed in Tyr bands both in IR and Raman spectra. This study may contribute to gain insight into the different biological performances of the EAK16‐derived peptides and to identify the most adequate materials usable for bone regeneration. Copyright © 2013 John Wiley & Sons, Ltd.

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“…As a consequence, the curve fitting procedure cannot give the absolute content of a structure. However, the curve fitting analysis may be of value in probing the nature and the extent of structural changes in proteins induced by external factors interacting with protein molecules, such as free radical attack or heating treatment [17,28].…”

Section: Raman Spectroscopymentioning

confidence: 99%

Metal ions modulate thermal aggregation of beta-lactoglobulin: A joint chemical and physical characterization

Navarra

Tinti

Foggia

et al. 2014

Journal of Inorganic Biochemistry

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Molecular basis of the role played by Cu(2+) and Zn(2+) ions during the thermal aggregation processes of beta-lactoglobulin (BLG) was studied by using a joint application of different techniques. In particular, Raman spectroscopy was very useful in identifying the different effects caused by the two metals at molecular level (i.e. changes in His protonation state, disulfides bridge conformation, and micro-environment of aromatic residues), evidencing the primary importance of the protein charge distribution during the aggregation process. Both metal ions are able to act on this factor and favor the protein aggregation, but Zn(2+) is able to alter the natural conformational state of BLG, causing a slight unfolding, whereas Cu(2+) ions play a role only during the thermal treatment. Thus, Zn(2+) ions favor the formation of bigger aggregates and branched fibril-like structures, whereas for Cu(2+) ions a greater number of cross-beta structures during thermal incubation and finally, fibrillar structures. The aggregation process occurs in two phases, as suggested by the measurements on the time evolution of the BLG aggregates: the first one is characterized by a partial unfolding of the protein and aggregate growth, forming oligomers and protofibrils, whereas the second one is characterized by further supramolecular assembly, leading to the formation of fibrils.

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Use of Raman spectroscopy for the identification of radical-mediated damages in human serum albumin

Cited by 26 publications

References 58 publications

Formation and Stabilization of Gold Nanoparticles in Bovine Serum Albumin Solution

Formation and Stabilization of Gold Nanoparticles in Bovine Serum Albumin Solution

Spectroscopic investigation on the structural modifications induced by radical stress on oligopeptides for tissue engineering

Metal ions modulate thermal aggregation of beta-lactoglobulin: A joint chemical and physical characterization

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