ABSTRACT
Ferula hermonis, a well-known species of the genus Ferula found in Lebanon and Syria, has a brilliant history in traditional medicine as it has been used for the treatment of erectile dysfunction in men and menopausal disturbances in women. Thanks to modern pharmacological and clinical investigations, F. hermonis is a valuable medicinal and condimental plant that may be used for the treatment of impotence and diabetes, the prevention of osteoporosis, and possesses anti-microbial and anti-inflammatory properties. Phytochemical investigations have shown that this plant contains daucane aryl esters such as ferutinin, which has exhibited various biological activities including hypoglycemic and estrogenic activities. Ferutinin is one of the strongest natural phytoestrogen which has agonistic activity on estrogen receptors, particularly α receptor. It seems that ferutinin and its derivatives play an important role in F. hermonis biological activities, mainly the beneficial effects of this plant on impotence, diabetes and osteoporosis. The present review discusses the available data on the active constituents and biological activities of F. hermonis and their possible underlying mechanisms of action.
Subject(s)
Ferula/chemistry , Plant Extracts/pharmacology , Plant Extracts/therapeutic use , Benzoates/analysis , Benzoates/pharmacology , Benzoates/therapeutic use , Bridged Bicyclo Compounds/analysis , Bridged Bicyclo Compounds/pharmacology , Bridged Bicyclo Compounds/therapeutic use , Cycloheptanes/analysis , Cycloheptanes/pharmacology , Cycloheptanes/therapeutic use , Humans , Plant Roots/chemistry , Sesquiterpenes/analysis , Sesquiterpenes/pharmacology , Sesquiterpenes/therapeutic useABSTRACT
Ferula persica, is the well-known species of the genus Ferula in Iran and has two varieties: persica and latisecta. They have both been extensively used in traditional medicine for a wide range of ailments. A great number of chemical compounds including sesquiterpene coumarins and polysulfides have been isolated from this plant. Fresh plant materials, crude extracts and isolated components of F. persica have shown a wide spectrum of pharmacological properties including anti-pigmentation in Serratia marcescens, cytotoxic, antibacterial, anti-fungal, anti-leishmanial, cancer chemopreventive, reversal of multi-drug resistance, anti-inflammatory and lipoxygenase inhibitory activity. The present review summarizes the data available regarding the chemical constituents and biological activities of F. persica.
ABSTRACT
Holo transferrin (TF) and the natural complex of human serum albumin and protoporphyrin IX (HSA-PPIX) are two serum carrier proteins that can interact with each other. Such an interaction may alter their binding sites. In this study, fluorescence spectroscopy, as well as zeta potential and molecular modeling techniques, have been used to compare the complexes (HSA-PPIX)-LMF and [(HSA-PPIX)-TF]-LMF. The Ka1, Ka2, values of (HSA-PPIX)-LMF and [(HSA-PPIX)-TF]-LMF were 1.1×10(5) M(-1), 9.7×10(6) M(-1), and 2.0×10(4) M(-1), 1.8×10(5) M(-1), respectively, and the n1, n2 values were respectively 1.19, 1.53 and 1.17, 1.65. The second derivative of the Trp emission scan of (HSA-PPIX)-LMF exhibited one negative band at 310 nm, whereas for the [(HSA-PPIX)-TF]-LMF system, we observed one negative band at 316 nm indicating an increase in polarity around Trp. The effect of TF on the conformation of (HSA-PPIX)-TF was analyzed using three-dimensional fluorescence spectroscopy. The phase diagram indicated that the presence of a second binding site on HSA and TF was due to the existence of intermediate structures. Zeta potential analysis showed that the presence of TF increased the positive charges of the HSA-PPIX system. Site marker experiments revealed that the binding site of LMF to HSA-PPIX changed from Sudlow's site IIA to Sudlow's site IIIB in the presence of TF. Moreover, molecular modeling studies suggested the sub-domain IIIB in HSA as the candidate place for the formation of the binding site of LMF on the (HSA-PPIX)-TF complex.
Subject(s)
Anti-Bacterial Agents/metabolism , Fluoroquinolones/metabolism , Protoporphyrins/metabolism , Serum Albumin/metabolism , Transferrin/metabolism , Anti-Bacterial Agents/chemistry , Fluoroquinolones/chemistry , Humans , Models, Molecular , Molecular Conformation , Multiprotein Complexes/chemistry , Multiprotein Complexes/metabolism , Protein Binding , Protoporphyrins/chemistry , Serum Albumin/chemistry , Spectrometry, Fluorescence/methods , Transferrin/chemistryABSTRACT
Human serum albumin (HSA) and holo transferrin (TF) are two serum carrier proteins that are able to interact with each other, thereby altering their binding behavior toward their ligands. During the course of this study, the interaction between HSA-PPIX and TF, in the presence and absence of lomefloxacin (LMF), was for the first time investigated using different spectroscopic and molecular modeling techniques. Fluorescence spectroscopy experiments were performed in order to study conformational changes of proteins. The RLS technique was utilized to investigate the effect of LMF on J-aggregation of PPIX, which is the first report of its kind. Our findings present clear-cut evidence for the alteration of interactions between HSA and TF in the presence of PPIX and changes in drug-binding to HSA and HSA-PPIX complex upon interaction with TF. Moreover, molecular modeling studies suggested that the binding site for LMF became switched in the presence of PPIX, and that LMF bound to the site IIA of HSA. The obtained results should give new insight into research in this field and may cast some light on the dynamics of drugs in biological systems.