Antiretrovirally Active Drug Hypericin Binds the IIA Subdomain of Human Serum Albumin:  Resonance Raman and Surface-Enhanced Raman Spectroscopy Study

Miškovský, Pavol; Jancura, Daniel; Sánchez-Cortés, Santiago; Kočišová, Eva; Chinsky, L.

doi:10.1021/ja974233a

Cited by 79 publications

(86 citation statements)

References 37 publications

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“…These techniques could show promise for real-time non-destructive monitoring of fluid or solid products during processing, but research on the feasibility and scope of these techniques for milk and milk product analysis is still in its infancy. Moreover, surface-enhanced Raman spectroscopy [26], vibrational Raman optical activity [22], surface plasmon resonance near-infrared spectroscopy [13] or femtosecond stimulated Raman spectroscopy [15] are examples of many recent developments in the paradigm of vibrational spectroscopy which have yet to be explored for detailed structural investigations of proteins and other constituents in dairy systems.…”

Section: Other Applications New Techniques and Trends In Vibrationalmentioning

confidence: 99%

Vibrational spectroscopy applied to the study of milk proteins

Li‐Chan¹

2007

Lait

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-Vibrational spectroscopy is a versatile tool for analysis of foods including dairy products. This paper provides an overview of techniques that may be useful to study structural properties and interactions of milk proteins. Specific examples of recent research conducted in our laboratory using Raman, micro-Raman and FT-Raman spectroscopy will be described to illustrate their applications for investigating protein-protein, protein-lipid, and protein-polysaccharide interactions, and for elucidating structure-function relationships of whey proteins and peptides. Raman spectroscopy was used to discriminate between structural changes of β-lactoglobulin in transparent fine-stranded versus particulate gels. Formation of particulate gel structures led to a more hydrophilic or exposed microenvironment around tryptophan residues, compared to a more hydrophobic microenvironment in translucent gels. A decrease in the α-helical content was more pronounced in translucent gels, while both types of gels retained considerable β-sheet structures, consistent with the known heat-resistance of the β-barrel structure of β-lactoglobulin. Principal component similarity analysis demonstrated that heat treatment and heat-κ-carrageenan interactions were the most influential factors affecting whey protein structure as monitored by spectral changes. Raman micro-spectroscopy was applied to investigate protein-lipid interactions at the interface between bovine serum albumin solution and mineral or corn oil. While Raman bands assigned to aromatic and aliphatic residues inferred involvement of hydrophobic interactions at the oil-water interface, the secondary structure was not significantly altered. Temperature-dependent changes in the Raman C-H stretching region of liposomes composed of phospholipids with varying headgroups and acyl chains were influenced by the presence of bovine lactoferricin. This approach may be useful to elucidate the interactions of cationic antimicrobial peptides with bacterial versus host cell membranes. A diverse range of other applications as well as new developments in techniques are emerging in the literature, indicating the potential for increasing use of vibrational spectroscopy in the analysis of milk and milk products. Résumé -Spectroscopie vibrationnelle appliquée à l'étude des protéines. La spectroscopie vibrationnelle est un outil adéquat pour l'analyse des aliments, dont des produits laitiers. Cet article présente une revue des techniques qui peuvent être utiles pour étudier les propriétés structurales et les interactions entre protéines laitières. Des exemples spécifiques de recherches récentes conduites dans notre laboratoire utilisant la spectroscopie Raman, micro-Raman et FT-Raman sont décrites pour illustrer leurs applications dans l'étude des interactions protéines/protéines, protéines/lipides et protéines/polysaccharides, et dans l'élucidation des relations structure/fonction des protéines et peptides du lactosérum. La spectroscopie Raman a été utilisée pour faire la distinction entre les c...

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Section: Other Applications New Techniques and Trends In Vibrationalmentioning

confidence: 99%

Vibrational spectroscopy applied to the study of milk proteins

Li‐Chan¹

2007

Lait

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“…23 On the other hand, the comparison with the SERS spectra of the same molecule at acidic pH [Figs 3(c), 4(c) Figs 3(d) and 4(d)] reveals clear differences of the ligand in the complex with respect to the free one, which mainly involve the keto and the adjacent OH groups, and which are related to the formation of H-bonds with H donors existing in the latter cavity as also found for hypericin. 5,6 The results obtained in this work demonstrate the existence of several differences between HSA f and BSA f concerning the binding of the studied drugs. It is usually accepted that the binding properties of site II (in subdomain IIIA) are essentially the same irrespective of the origin of the albumin because the amino acid sequence of the subdomain, mainly the amino acids in direct contact with the ligand, is greatly conserved in all mammalian albumins.…”

Section: Discussionmentioning

confidence: 54%

“…A previous study of this molecule at different pH values was carried out in order to relate the interaction of this molecule with the proteins with possible changes in the protonation state of the ligand, as was also observed for other similar molecules. 5,16 More details about the acidic behaviour of DT and QZ on Ag colloids will be published elsewhere. 17 In the SERS spectrum of DT at pH 3.5 [ Fig.…”

Section: Mico-sers Of Danthronmentioning

confidence: 99%

“…In recent works we studied the interaction between the related molecule hypericin and serum albumins of different origins (human, rat and bovine) by Raman spectroscopy. 5,6 Serum albumin as the most abundant plasma protein contributes significantly to many transport and regulatory processes. The protein binds a wide variety of substrates such as metals, fatty acids, amino acids, hormones and large range of therapeutic drugs.…”

Section: Introductionmentioning

confidence: 99%

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Joint application of micro‐Raman and surface‐enhanced Raman spectroscopy to the interaction study of the antitumoral anthraquinone drugs danthron and quinizarin with albumins

Fabriciová

Sánchez-Cortés

Garcia-Ramos

et al. 2004

J Raman Spectroscopy

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We report on the joint application of surface-enhanced Raman scattering (SERS) and micro-Raman techniques to the study of danthron (DT) and quinizarin (QZ) and their complexes with human and bovine albumins. We propose a novel method based on the combination of SERS and micro-Raman spectroscopy by using immobilized Ag nanoparticles, which we have named micro-SERS, to improve the sensitivity of the SERS technique and that could be applied in recognition processes of drugs with large biomolecules. The micro-SERS technique demonstrated clear advantages over direct measurements in air: reproducibility, rapidity and high sensitivity due to a large coverage of the metal surface and good organization of the adsorbate on the surface. Furthermore, the chemical damage of the analyte induced by laser irradiation is substantially reduced. By means of this method, we were able to deduce important information concerning the binding properties of DT and QZ when interacting with human and bovine albumins. For instance, the interaction mechanism can be drastically modified when fatty acids are present in albumins, there are large differences between human and bovine albumins in the binding of the studied drugs related to changes in the amino-acid sequence of the binding pockets of these proteins and the interaction mechanism of the analysed drugs can be different depending on their structure.

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“…However, under physiologic conditions, bilirubin IX (2) will also be present, and as with 1 it will be mostly found selectively bound (K f % 10 7 ) to the active site of the subdomain IIA of serum albumin [10,11]. The two binding regions are closely spaced [10,12]; it may therefore be anticipated that if the two pigments are simultaneously bound to albumin they could interact upon the in¯uence of light. Since 2 is known to vividly undergo reactions with singlet oxygen or radicals of 1 [13], this could have implications for the use of 1 in phototherapy and photdynamic therapy.…”

Section: Introductionmentioning

confidence: 99%

Concerning the Hypericin Sensitized Photooxidation of Bilirubin IXα

Hagenbuchner

Falk

1999

Monatshefte fuer Chemie

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In aerated protic solvents like ethanol or 80% aqueous ethanol, bilirubin IX was found to undergo a hypericin sensitized oxidative photodestruction. By means of quenching experiments it was deduced that this was mainly due to the sensitized production of singlet oxygen, but also to some extent to the sensitized formation of superoxide radicals which then react with bilirubin IX. In absence of oxygen, a photochemically induced disproportionation reaction of hypericin may lead to the oxidative degradation of bilirubin IX. Upon selective binding of the two pigments to human serum albumin the photosensitized bilirubin IX destruction was found to be compeletely retarded. Accordingly, the presence of bilirubin IX within the realm of hypericin assisted photodynamic therapy should have no adverse effects, and neonatal jaundice phototherapy would not bene®t from an administration of hypericin.

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Antiretrovirally Active Drug Hypericin Binds the IIA Subdomain of Human Serum Albumin: Resonance Raman and Surface-Enhanced Raman Spectroscopy Study

Cited by 79 publications

References 37 publications

Vibrational spectroscopy applied to the study of milk proteins

Vibrational spectroscopy applied to the study of milk proteins

Joint application of micro‐Raman and surface‐enhanced Raman spectroscopy to the interaction study of the antitumoral anthraquinone drugs danthron and quinizarin with albumins

Concerning the Hypericin Sensitized Photooxidation of Bilirubin IXα

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