TY - JOUR
T1 - The complex of hypericin with β-lactoglobulin has antimicrobial activity with potential applications in dairy industry
AU - Rodríguez-Amigo, Beatriz
AU - Delcanale, Pietro
AU - Rotger, Gabriel
AU - Juárez-Jiménez, Jordi
AU - Abbruzzetti, Stefania
AU - Summer, Andrea
AU - Agut, Montserrat
AU - Luque, F. Javier
AU - Nonell, Santi
AU - Viappiani, Cristiano
N1 - Funding Information:
Financial support for this research was obtained from the Spanish MINECO ( CTQ2013-48767-C3-1-R; SAF2011-27642 ), Generalitat de Catalunya ( 2014SGR304 and 2014SGR1189 ; ICREA Academia), and from Ministero degli Affari Esteri, Direzione generale per la promozione del sistema Paese (Progetti di Grande Rilevanza, Italia-Argentina 2011–2013). J.Juárez-Jiménez thanks Instituto de Salud Carlos III for FIS fellowship. The Consorci de Serveis Universitaris de Catalunya is acknowledged for computational facilities.
Publisher Copyright:
© 2015 American Dairy Science Association.
PY - 2015/1/1
Y1 - 2015/1/1
N2 - Using a combination of molecular modeling and spectroscopic experiments, the naturally occurring, pharmacologically active hypericin compound is shown to form a stable complex with the dimeric form of β-lactoglobulin (β-LG). Binding is predicted to occur at the narrowest cleft found at the interface between monomers in the dimeric β-LG. The complex is able to preserve the fluorescence and singlet oxygen photosensitizing properties of the dye. The equilibrium constant for hypericin binding has been determined as Ka = 1.40 ± 0.07μM-1, equivalent to a dissociation constant, Kd = 0.71 ± 0.03μM. The complex is active against Staphylococcus aureus bacteria. Overall, the results are encouraging for pursuing the potential application of the complex between hypericin and β-LG as a nanodevice with bactericidal properties for disinfection.
AB - Using a combination of molecular modeling and spectroscopic experiments, the naturally occurring, pharmacologically active hypericin compound is shown to form a stable complex with the dimeric form of β-lactoglobulin (β-LG). Binding is predicted to occur at the narrowest cleft found at the interface between monomers in the dimeric β-LG. The complex is able to preserve the fluorescence and singlet oxygen photosensitizing properties of the dye. The equilibrium constant for hypericin binding has been determined as Ka = 1.40 ± 0.07μM-1, equivalent to a dissociation constant, Kd = 0.71 ± 0.03μM. The complex is active against Staphylococcus aureus bacteria. Overall, the results are encouraging for pursuing the potential application of the complex between hypericin and β-LG as a nanodevice with bactericidal properties for disinfection.
KW - Antimicrobial
KW - Hypericin
KW - Photosensitizer
KW - β-lactoglobulin
UR - http://www.scopus.com/inward/record.url?scp=84918808797&partnerID=8YFLogxK
U2 - 10.3168/jds.2014-8691
DO - 10.3168/jds.2014-8691
M3 - Article
C2 - 25465550
AN - SCOPUS:84918808797
SN - 0022-0302
VL - 98
SP - 89
EP - 94
JO - Journal of Dairy Science
JF - Journal of Dairy Science
IS - 1
ER -