BODIPY(aryl)iodonium salts in the efficient synthesis of diversely functionalized BODIPYs and selective detection of serum albumin.

BODIPY(aryl)iodonium salts were readily accessible from the high-yielding reaction of BODIPY with iodoarenes or hydroxyl(tosyloxy)iodoarenes in the presence of m-CPBA. The prepared BODIPY(aryl)iodonium salts bearing substituents of varied electronic nature were utilized for the direct syntheses of thiocyanate, azide, amine and acrylate functionalized BODIPYs and ß,ß'-bis-BODIPYs. The regioselective syntheses of α-piperidinyl and ß-piperidinyl substituted BODIPYs were achieved through the reaction of BODIPY(aryl)iodonium salts with piperidine in the absence and presence of copper(I). Expeditious and high yielding (79-82%) synthesis of ß,ß'-bis-BODIPYs was also developed through the palladium-catalyzed reductive coupling of the easily accessible BODIPY(aryl)iodonium salts. Some of the indole-appended BODIPYs and bis-BODIPYs displayed strong absorption in the visible region (∼610 nm). The BODIPY(aryl)iodonium salts also showed significant binding with serum albumin and were observed to be selective serum protein sensors with estimated limits of detection as low as 7 µg mL-1 in some cases.

Exploring the impact of novel thiazole-pyrazole fused benzo-coumarin derivatives on human serum albumin: Synthesis, photophysical properties, anti-cholinergic activity, and interaction studies.

Derivatives of thiazole-pyrazole fused benzo-coumarin compounds were successfully synthesized and characterized, followed by a comprehensive spectroscopic investigation on various photophysical properties in different media. The multipronged approach using steady state and time resolved fluorescence spectroscopy pointed out the impact of substitution in the estimated spectroscopic and other physicochemical properties of the systems. Further, the evaluation of anti-acetylcholinesterase (anti-AChE) activity yielded significant insight into the therapeutic potential of the synthesized coumarinyl compounds for the treatment of Alzheimer's disease (AD). The findings revealed a non-competitive mode of inhibition mechanism, with an estimated IC50 value of 67.72 ± 2.00 nM observed for one of the investigated systems as AChE inhibitor. Notably, this value is even lower than that of an FDA-approved AD drug Donepezil (DON), indicating the enhanced potency of the coumarin derivatives in inhibiting AChE. Interestingly, significant diminution in inhibition was observed in presence of human serum albumin (HSA) as evidenced by the relative increase in IC50 value by 8 âˆ¼ 39 % in different cases, which emphasized the role of albumin proteins to control therapeutic efficacies of potential medications. In-depth spectroscopic and in-silico analysis quantified the nature of interactions of the investigated systems with HSA and AChE. Overall, the outcomes of this study provide significant understanding into the biophysical characteristics of novel thiazole-pyrazole fused benzo-coumarin systems, which could aid in the development of new cholinergic agents for the treatment of AD and materials based on coumarin motifs.

Deciphering the interactions of phytochemicals with ovalbumin, the major food allergen from egg white: spectroscopic and computational studies.

Ovalbumin (OVA), the major component of egg white, has been used as a model carrier protein to study the interaction of four bioactive phytochemicals 6-hydroxyflavone, chrysin, naringin, and naringenin. A static quenching mechanism was primarily associated with the complexation of the flavonoids with OVA. Hydrophobic forces play a major part in the stability of the complexes. The structural changes within the protein in response to flavonoid binding revealed a decrease in OVA's α-helical content. The hypothesized binding site for flavonoids in OVA overlaps with one or more immunoglobulin E-binding epitopes that may have some effect in the immunoglobulin E response pathway. The flavonoids remain in the same binding site throughout the simulation time and impart protein stability by forming different noncovalent interactions. This study presents comprehensive information about the interaction of the flavonoids with OVA and the associated structural variations after the binding, which might help researchers better comprehend similar medication pharmacodynamics and provide critical information for future therapeutic development.

Iodine(III)-promoted regioselective and efficient synthesis of ß-triazolyl BODIPYs for the selective recognition of nickel ions and bovine serum albumin.

Various ß-triazolyl tethered BODIPYs were efficiently prepared in a sequential one-pot protocol involving the initial reaction of BODIPY with iodobenzene diacetate (IBD) and sodium azide to in situ generate BODIPY azides followed by a copper-catalyzed azide-alkyne cycloaddition reaction. Under the optimized reaction conditions, various ß-triazolyl BODIPYs 5a-i were successfully prepared in good yields and adequately characterized by using UV, NMR, mass spectral data and XRD analyses. The UV-Visible spectra of the prepared ß-triazolyl BODIPYs 5a-i showed intense absorption bands (514-545 nm) with a 13-44 nm red shift when compared with those of the parent BODIPY. The selective recognition of compound 5d towards Ni2+ ions (detection limit 0.26 nM) led to significant quenching in the fluorescence intensity over other selected bivalent metal ions. The complex formed between 5d and Ni2+ in a stoichiometry of 2 : 1 was found to have a binding constant of 7.5 × 105 M-1. The fluorescence of compound 5i gets enhanced gradually upon interaction with bovine serum albumin due to its selective and high binding affinity (1.25 × 105 M-1) with protein and a concomitant decrease in the total non-radiative decay rate.

Chlorin e6 decorated doxorubicin encapsulated chitosan nanoparticles for photo-controlled cancer drug delivery.

In the study we have reported the physico-chemical, photophysical and morphological properties of chlorin e6 (Ce6) decorated doxorubicin (DOX) encapsulated chitosan (CS)-tripolyphosphate (TPP) nanoparticles which prepared by ionotropic gelation method. The Ce6 physically loaded onto the nanoparticles by self-assembly of CS with TPP-DOX under aqueous conditions. The results from DLS studies highlights the prepared nanoparticles that possess the size in the range of 80-120 nm. with negatively charged of -6 mV. The SEM and AFM images showed 80-120 nm size while the average size of the Ce6 decorated nanoparticles was found to be around 100-130 nm. The absorption spectra of Ce6 decorated nanoparticles are similar when compared to free Ce6 which suggest there is no change in the Ce6 chromophore upon decoration. This nanoparticle showed high photostability and singlet oxygen generation (SOG). The Ce6 decorated and DOX encapsulated nanoparticles sizes and charges are in the range of 90-130 nm and -30 mV respectively. The nanoparticles showed high encapsulation efficiency towards DOX as well as pH controlled release. This has significant anti-proliferative activity against MCF-7 breast cancer cells after irradiation at near infra-red (NIR) ranges were evaluated. This could have potential applications in photo-controlled smart DOX delivery system for cancer treatment.

Design of biostable scaffold based on collagen crosslinked by dialdehyde chitosan with presence of gallic acid.

In this study, we have prepared the biostable collagen scaffold which is crosslinked by dialdehyde chitosan (DAC) with presence of Gallic acid (GA) and characterized its physico-chemical, biostable and biocompatible properties. The digital photographic and scanning electron microscopic (SEM) images of the prepared collagen scaffold is exposed well with properly oriented interconnected porous natured structure. The appearance of diffraction peaks showed slightly crystalline characteristic when compared to others. The differential scanning calorimetric (DSC) and thermogravimetric analysis (TGA) measurements indicates well significantly increased denaturation temperature (TD) and decreased decomposition rate. FT-IR result suggests the structural integrity of collagen which favours the molecular stability. The dialdehyde groups from DAC crosslinked with collagen functional groups that increase the molecular crosslinking owing to the large number of amino groups in its molecular chain. This scaffold exhibited 87% resistance against collagenolytic degradation by collagenase. The results showed that the improved biostability which prevents the free access of the collagenase to binds with the collagen triple helical chains. This scaffold confirm high biocompatibilities; enhanced cell proliferation and adhesions properties. This results gains new insight into the collagen scaffold to improves the biostability. This could be suitable method to preparation of collagenous biomaterials for tissue engineering applications.