Silver nanoparticle modulates the aggregation of beta-lactoglobulin and induces to form rod-like aggregates

Sardar, Subrata; Anas, Md; Maity, Sanhita; Pal, Sampa; Parvej, Hasan; Begum, Shahnaz; Dalui, Ramkrishna; Sepay, Nayim; Halder, Umesh Chandra

doi:10.1016/j.ijbiomac.2018.12.039

Cited by 10 publications

(5 citation statements)

References 59 publications

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“…Thioflavin T (Th-T), a benzothiazole dye, is a good fluorescent ligand that selectively binds with the hydrophobic site of the fibrillar aggregates of the protein leading to an increase in fluorescence intensity at around 480 nm upon excitation at 480 nm. 23 Upon heating at 78 °C, the native β-lg gets aggregated which can be measured in terms of intensity of the Th-T spectra. Here, all the other heat-treated β-lg samples with different coumarin derivatives produced different Th-T emission intensities which are proportional to the amount of aggregates formed in the different protein solutions.…”

Section: Resultsmentioning

confidence: 99%

Coumarin derivatives inhibit the aggregation of β-lactoglobulin

et al. 2022

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Section: Resultsmentioning

confidence: 99%

Coumarin derivatives inhibit the aggregation of β-lactoglobulin

et al. 2022

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“…ANS is a molecule with both hydrophilic and hydrophobic properties, which is an excellent tool to reflect ligand–protein interactions via its fluorescence changes. , Usually, BLG can possess two binding sites for ANS: an external site that is close to a hydrophobic patch on the protein surface and an internal site that is located in the hydrophobic β-barrel of the protein. , Herein, ANS (120 μM) was used to further characterize the hydrophobic interactions in the formations of the HP-BLG complex and PPIX-BLG complex. The solution of each group was excited at 380 nm, and the emission spectra of wavelength at 400–600 nm were recorded.…”

Section: Resultsmentioning

confidence: 99%

Spectroscopic and Theoretical Investigation of β-Lactoglobulin Interactions with Hematoporphyrin and Protoporphyrin IX

et al. 2021

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Hematoporphyrin (HP) and protoporphyrin IX (PPIX) are useful porphyrin photosensitizers with significant application values in photodynamic therapy. Currently, many strategies have been developed to improve their clinical performance, such as incorporating them with nanoparticle (NP) carriers. In this work, we studied the possibility of using β-lactoglobulin (BLG) as a potential NP carrier due to their hydrophobic affinity, pH sensitivity, and low cost of extraction and preservation. The interaction mechanisms of BLG with HP and PPIX were investigated using spectroscopic techniques and molecular docking methods. The molecular docking results agree well with the experimental results, which demonstrate that the formations of HP-BLG and PPIX-BLG complexes are endothermic processes and the main acting force is hydrophobic force. Furthermore, the opening–closure states of EF loop have a great influence on the HP-BLG complex formation, where the central hydrophobic cavity of β-barrel is available for HP binding at pH 7.4 but not available at pH 6.2. However, the formation of the PPIX-BLG complex is less dependent on the states of the EF loop, and the binding sites of PPIX are both located on the external surface of BLG under both pH 7.4 and 6.2 conditions. All of our results would provide new insight into the mechanisms of noncovalent interactions between BLG and HP/PPIX. It is believed that this work indicated the potential application values of BLG in designing pH-sensitive carriers for the delivery of HP and PPIX, as well as other poorly soluble drugs.

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“…This process of D 2 O exchange was repeated 3–4 times. 36 Finally, the D 2 O exchanged β-lg samples were placed between two CaF 2 windows separated by a 50 μm thick Teflon spacer. FTIR scans were collected in the range of 1400–1800 cm −1 at a resolution of 2 cm −1 in N 2 environment using a Spectrum 100 FTIR spectrometer (PerkinElmer).…”

Section: Methodsmentioning

confidence: 99%