222
Views
6
CrossRef citations to date
0
Altmetric
Research Article

Interaction between the photosensitizer lumichrome and human serum albumin: effect of excipients

&
Pages 992-1000 | Received 15 Apr 2016, Accepted 02 Jun 2016, Published online: 27 Jul 2016

References

  • Ahmad I, Fasihullah Q, Vaid FH. A study of simultaneous photolysis and photoaddition reactions of riboflavin in aqueous solution. J Photochem Photobiol B 2004;75:13–20.
  • Yamamoto K, Asano Y. Efficient production of lumichrome by Microbacterium sp. Strain TPU 3598. Appl Environ Microbiol 2015;81:7360–7367.
  • Tyagi A, Penzkofer A. Absorption and emission spectroscopic characterization of lumichrome in aqueous solutions. Photochem Photobiol 2011;87:524–533.
  • Marchena M, Gil M, Martin C, et al. Stability and photodynamics of lumichrome structures in water at different pHs and in chemical and biological caging media. J Phys Chem B 2011;115:2424–2435.
  • Cunningham O, Gore MG, Mantle TJ. Initial-rate kinetics of the flavin reductase reaction catalysed by human biliverdin-IXbeta reductase (BVR-B). Biochem J 2000;345:393–399.
  • Fieschi F, Nivière V, Frier C, et al. The mechanism and substrate specificity of the NADPH: flavin oxidoreductase from Escherichia coli. J Biol Chem 1995;270:30392–30400.
  • Bergh VJ, Bruzell E, Hegge AB, Tønnesen HH. Influence of formulation on photoinactivation of bacteria by lumichrome. Pharmazie 2015;70:574–580.
  • Hamblin MR, Hasan T. Photodynamic therapy: a new antimicrobial approach to infectious disease? Photochem Photobiol Sci 2004;3:436–450.
  • Jori G, Fabris C, Soncin M, et al. Photodynamic therapy in the treatment of microbial infections: basic principles and perspective applications. Lasers Surg Med 2006;38:468–481.
  • Ghafouri B, Tagesson C, Lindahl M. Mapping of proteins in human saliva using two-dimensional gel electrophoresis and peptide mass fingerprinting. Proteomics 2003;3:1003–1015.
  • Trengove NJ, Langton SR, Stacey MC. Biochemical analysis of wound fluid from nonhealing and healing chronic leg ulcers. Wound Repair Regen 1996;4:234–239.
  • Buchan IA, Andrews JK, Lang SM, et al. Clinical and laboratory investigation of the composition and properties of human skin wound exudate under semi-permeable dressings. Burns 1981;7:326–334.
  • He XM, Carter DC. Atomic structure and chemistry of human serum albumin. Nature 1992;358:209–215.
  • Fasano M, Curry S, Terreno E, et al. The extraordinary ligand binding properties of human serum albumin. IUBMB Life 2005;57:787–796.
  • Sudlow G, Birkett DJ, Wade DN. Further characterization of specific drug binding sites on human serum albumin. Mol Pharmacol 1976;12:1052–1061.
  • Sudlow G, Birkett DJ, Wade DN. The characterization of two specific drug binding sites on human serum albumin. Mol Pharmacol 1975;11:824–832.
  • Kragh-Hansen U, Chuang VT, Otagiri M. Practical aspects of the ligand-binding and enzymatic properties of human serum albumin. Biol Pharm Bull 2002;25:695–704.
  • Tesseromatis C, Alevizou A. The role of the protein-binding on the mode of drug action as well the interactions with other drugs. Eur J Drug Metab Pharmacokinet 2008;33:225–230.
  • Laza-Knoerr AL, Gref R, Couvreur P. Cyclodextrins for drug delivery. J Drug Target 2010;18:645–656.
  • Loftsson T, Brewster ME. Pharmaceutical applications of cyclodextrins. 1. Drug solubilization and stabilization. J Pharm Sci 1996;85:1017–1025.
  • Loftsson T, Masson M. Cyclodextrins in topical drug formulations: theory and practice. Int J Pharm 2001;225:15–30.
  • Knop K, Hoogenboom R, Fischer D, Schubert US. Poly(ethylene glycol) in drug delivery: pros and cons as well as potential alternatives. Angew Chem Int Ed Engl 2010;49:6288–6308.
  • Polyethylene glycol [MAK Value Documentation, 1998]. The MAK-Collection for Occupational Health and Safety. 10. Weinheim, Germany: Wiley-VCH Verlag GmbH & Co. KGaA; 2002.
  • Dumortier G, Grossiord JL, Agnely F, Chaumeil JC. A review of poloxamer 407 pharmaceutical and pharmacological characteristics. Pharm Res 2006;23:2709–2728.
  • Selva Sharma A, Anandakumar S, Ilanchelian M. A combined spectroscopic and molecular docking study on site selective binding interaction of Toluidine blue O with Human and Bovine serum albumins. J Lumin 2014;151:206–218.
  • Lakowicz JR. Principles of fluorescence spectroscopy. 3rd ed. New York: Springer; 2010.
  • Valeur B, Berberan-Santos MN. Molecular fluorescence. Principles and applications. 2nd ed. Weinheim, Germany: Wiley-VCH; 2013.
  • Hosainzadeh A, Gharanfoli M, Saberi M, Chamani J. Probing the interaction of human serum albumin with bilirubin in the presence of aspirin by multi-spectroscopic, molecular modeling and zeta potential techniques: insight on binary and ternary systems. J Biomol Struct Dyn 2012;29:1013–1050.
  • Terekhova IV, Kumeev RS, Alper GA, Agafonov AV. Thermodynamic characteristics of the formation of α- and β-cyclodextrin complexes with lumichrome, lumazine, and uracil in aqueous solution. Russ J Phys Chem A 2011;85:1844–1849.
  • Sarkar B, Das U, Bhattacharyya S, Bose SK. The quenching of lumichrome fluorescence by β-cyclodextrin: evidence for inclusion complex. Bull Chem Soc Jpn 1995;68:1807–1809.
  • Komasa J, Rychlewski J, Kozioł J. Electronic structure of alloxazine and its methyl derivatives. J Mol Struct (THEOCHEM) 1988;170:205–212.
  • Sun M, Moore TA, Song PS. Molecular luminescence studies of flavins. I. The excited states of flavins. J Am Chem Soc 1972;94:1730–1740.
  • Sikorska E, Khmelinskii IV, Prukała W, et al. Spectroscopy and photophysics of lumiflavins and lumichromes. J Phys Chem A 2004;108:1501–1508.
  • Maity B, Chatterjee A, Seth D. Effect of nano-confinement on the photophysics of lumichrome. Chem Phys Lett 2013;565:108–115.
  • Johnson CM. Differential scanning calorimetry as a tool for protein folding and stability. Arch Biochem Biophys 2013;531:100–109.
  • Lang BE, Cole KD. Unfolding properties of recombinant human serum albumin products are due to bioprocessing steps. Biotechnol Prog 2015;31:62–69.
  • Michnik A, Michalik K, Drzazga Z. DSC study of human serum albumin ageing processes in aqueous and low concentration ethanol solutions. Polish J Environ Stud 2006;15:81–83.
  • Farruggia B, Picó GA. Thermodynamic features of the chemical and thermal denaturations of human serum albumin. Int J Biol Macromol 1999;26:317–323.
  • Michnik A, Michalik K, Kluczewska A, Drzazga Z. Comparative DSC study of human and bovine serum albumin. J Therm Anal Calorim 2006;84:113–117.
  • Farruggia B, Rodriguez F, Rigatuso R, et al. The participation of human serum albumin domains in chemical and thermal unfolding. J Protein Chem 2001;20:81–89.
  • Ohtake S, Kita Y, Arakawa T. Interactions of formulation excipients with proteins in solution and in the dried state. Adv Drug Deliv Rev 2011;63:1053–1073.
  • Farruggia B, Nerli B, Di Nuci H, et al. Thermal features of the bovine serum albumin unfolding by polyethylene glycols. Int J Biol Macromol 1999;26:23–33.
  • Katakam M, Banga AK. Use of poloxamer polymers to stabilize recombinant human growth hormone against various processing stresses. Pharm Dev Technol 1997;2:143–149.
  • Yan J, Wu D, Ma X, et al. Spectral and molecular modeling studies on the influence of β-cyclodextrin and its derivatives on aripiprazole-human serum albumin binding. Carbohydr Polym 2015;131:65–74.
  • Gil M, Wang Y, Douhal A. Ultrafast dynamics of lumichrome in solution and in chemical and biological caging media. J Photochem Photobiol A Chem 2012;235:146–155.
  • Memarpoor-Yazdi M, Mahaki H. Probing the interaction of human serum albumin with vitamin B2 (riboflavin) and l-Arginine (l-Arg) using multi-spectroscopic, molecular modeling and zeta potential techniques. J Lumin 2013;136:150–159.
  • Nanda RK, Sarkar N, Banerjee R. Probing the interaction of ellagic acid with human serum albumin: a fluorescence spectroscopic study. J Photochem Photobiol A Chem 2007;192:152–158.
  • Sułkowska A. Interaction of drugs with bovine and human serum albumin. J Mol Struct 2002;614:227–232.
  • Zhao H, Ge M, Zhang Z, et al. Spectroscopic studies on the interaction between riboflavin and albumins. Spectrochim Acta A Mol Biomol Spectrosc 2006;65:811–817.
  • Matei I, Hillebrand M. Interaction of kaempferol with human serum albumin: a fluorescence and circular dichroism study. J Pharm Biomed Anal 2010;51:768–773.
  • Sengupta A, Sasikala WD, Mukherjee A, Hazra P. Comparative study of flavins binding with human serum albumin: a fluorometric, thermodynamic, and molecular dynamics approach. Chemphyschem 2012;13:2142–2153.
  • Natesan S, Sowrirajan C, Yousuf S, Enoch IV. Mode of encapsulation of linezolid by β-cyclodextrin and its role in bovine serum albumin binding. Carbohydr Polym 2015;115:589–597.
  • Wang L, Yan J, Li Y, et al. The influence of hydroxypropyl-β-cyclodextrin on the solubility, dissolution, cytotoxicity, and binding of riluzole with human serum albumin. J Pharm Biomed Anal 2016;117:453–463.
  • Vukićević M, Tønnesen HH. Interaction between curcumin and human serum albumin in the presence of excipients and the effect of binding on curcumin photostability. Pharm Dev Technol 2016;21:428–436.
  • Esmaeilzadeh S, Valizadeh H, Zakeri-Milani P. The effects of pH, temperature and protein concentration on the in vitro binding of flutamide to human serum albumin. Pharm Dev Technol 2016. [Epub ahead of print]. doi: 10.3109/10837450.2016.1163392.
  • Liu Y, Liu Y, Guo R. Effect of cyclodextrins on the interaction between BSA and sodium dodecyl benzene sulfonate. J Solution Chem 2011;40:1140–1152.
  • Kurkov SV, Loftsson T, Messner M, Madden D. Parenteral delivery of HPβCD: effects on drug-HSA binding. AAPS PharmSciTech 2010;11:1152–1158.
  • Remucal CK, McNeill K. Photosensitized amino acid degradation in the presence of riboflavin and its derivatives. Environ Sci Technol 2011;45:5230–5237.
  • Huang R, Kim HJ, Min DB. Photosensitizing effect of riboflavin, lumiflavin, and lumichrome on the generation of volatiles in soy milk. J Agric Food Chem 2006;54:2359–2364.
  • Glass BD, Brown ME, Daya S, et al. Influence of cyclodextrins on the photostability of selected drug molecules in solution and the solid-state. Int J Photoenergy 2001;3:205–11.
  • Loukas YL, Jayasekera P, Gregoriadis G. Novel liposome-based multicomponent systems for the protection of photolabile agents. Int J Pharm 1995;117:85–94.
  • Hegge AB, Bruzell E, Kristensen S, Tønnesen HH. Photoinactivation of Staphylococcus epidermidis biofilms and suspensions by the hydrophobic photosensitizer curcumin – effect of selected nanocarrier. Studies on curcumin and curcuminoides XLVII. Eur J Pharm Sci 2012;47:65–74.
  • Vorobey P, Steindal AE, Off MK, et al. Influence of human serum albumin on photodegradation of folic acid in solution. Photochem Photobiol 2006;82:817–822.
  • Pattison DI, Rahmanto AS, Davies MJ. Photo-oxidation of proteins. Photochem Photobiol Sci 2012;11:38–53.
  • Davies MJ. Reactive species formed on proteins exposed to singlet oxygen. Photochem Photobiol Sci 2004;3:17–25.
  • Hegge AB, Andersen T, Melvik JE, et al. Formulation and bacterial phototoxicity of curcumin loaded alginate foams for wound treatment applications: studies on curcumin and curcuminoides XLII. J Pharm Sci 2011;100:174–185.

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.