Binding of Cationic Lipids to Milk β-Lactoglobulin

Hasni, Imed; Bourassa, P.; Tajmir-Riahi, H.A.

doi:10.1021/jp200045h

Cited by 48 publications

(34 citation statements)

References 34 publications

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“…Increase in the intensity of Amide I and Amide II indicated the binding of DIM to the β-LG. Similar results were obtained by Hasni et al [24] who found the increase in the intensity of Amide I and Amide II but no major shifting after the binding of lipid to β-LG. Both Amide I and Amide II are sensitive to the change of secondary structure [40].…”

Section: Resultssupporting

confidence: 90%

“…C=O, N–H, C–N are often involved in the hydrophilic interaction and form hydrogen bonds. The absorption band in the region of 2800 to 3000 cm −1 is attributed to –C–H antisymmetric stretching vibration and is also involved in hydrophobic interaction [24]. Changes in the intensity indicated the involvement of hydrophobic interaction in the β-LG and DIM complexes.…”

Section: Resultsmentioning

confidence: 99%

“…β-LG is a good encapsulating system for nutraceuticals [22]. Whey protein as a carrier can improve the bioactivity of hydrophobic ligands by improving the stability of ligands [23] or in vivo transfer efficiency [16,24]. In addition, β-LG is a well-known food allergen and studies have shown that binding of β-LG to a number of compounds could play a coadjutant role in the onset of immune responses and reducing allergy [25,26].…”

Section: Introductionmentioning

confidence: 99%

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Interactions between β-Lactoglobulin and 3,3′-Diindolylmethane in Model System

et al. 2019

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The compound 3,3′-diindolylmethane (DIM) has a broad spectrum of anticancer activities. However, low stability and bioavailability limit its application. Elucidating interactions between DIM and β-lactoglobulin (β-LG) may be useful for fabricating whey protein-based protecting systems. Interaction with DIM increased the diameter and absolute zeta potential value of β-LG. UV-absorption spectra suggested that there was a complex of DIM and β-LG. β-LG showed enhanced fluorescence intensity by complexing with DIM with a binding constant of 6.7 × 105 M−1. Upon interaction with DIM, β-LG was decreased in secondary structure content of helix and turn while increased in β-sheet and unordered. FT-IR spectra and molecular docking results indicated the roles of hydrophobic interaction and hydrogen bond for the formation of DIM and β-LG nanocomplexes. Data suggested that β-LG may be a good vehicle for making a protein-based DIM protection and delivery system due to the tight binding of DIM to β-LG.

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Section: Resultssupporting

confidence: 90%

Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Interactions between β-Lactoglobulin and 3,3′-Diindolylmethane in Model System

et al. 2019

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“…site, although the shifts themselves were only slight. β-Lactoglobulin has only 2 Trp residues, corresponding to the Trp19 and Trp61 residues in its AA sequence (Barbiroli et al, 2011;Hasni et al, 2011). The Trp19 residue is located at the bottom of the protein β-barrel and contributes to 80% of the total fluorescence of β-LG (Hasni et al, 2011).…”

Section: Discussionmentioning

confidence: 99%

“…β-Lactoglobulin has only 2 Trp residues, corresponding to the Trp19 and Trp61 residues in its AA sequence (Barbiroli et al, 2011;Hasni et al, 2011). The Trp19 residue is located at the bottom of the protein β-barrel and contributes to 80% of the total fluorescence of β-LG (Hasni et al, 2011). In contrast, it has been reported that Trp61 is unlikely to have a significant effect on the fluorescence spectrum of β-LG, even if the protein structure were altered (Barbiroli et al, 2011).…”

Section: Discussionmentioning

confidence: 99%

Self-assembled β-lactoglobulin–oleic acid and β-lactoglobulin–linoleic acid complexes with antitumor activities

Fang

Zhang

Tian

et al. 2015

Journal of Dairy Science

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β-Lactoglobulin (β-LG) can bind to fatty acids such as oleic acid (OA) and linoleic acid (LA). Another whey protein, α-lactalbumin (α-LA), can also bind to OA to give the complex α-LA-OA, which has antitumor properties. Based on reports that the activity of α-LA-OA is highly dependent on OA, as well as the acquisition of similar complexes using other proteins, such as lysozyme and lactoferrin, we speculated whether β-LG could also kill tumor cells after binding to other fatty acids. Therefore, we prepared complexes of β-LG with OA (β-LG-OA) and LA (β-LG-LA) in the current study and evaluated them in terms of antitumor activity and thermostability using the methylene blue method and differential scanning calorimetry, respectively. The structural features of these complexes were also evaluated using fluorescence spectroscopy and circular dichroism. The binding dynamics of OA and LA to β-LG were studied using isothermal titration calorimetry. Cell viability results revealed that β-LG-LA and β-LG-OA exhibited similar antitumor activities. Interestingly, the binding of β-LG to LA led to an increase in its thermostability, whereas its binding to OA had very little effect. The environments of the tryptophan residues in the β-LG-OA and β-LG-LA complexes were very different, with the residues being blue- and red-shifted, respectively. Furthermore, the hydrophobic regions in β-LG were buried after binding of OA, which was slightly changed in β-LG-LA. Circular dichroism results showed that β-LG-OA enhanced the tertiary structure, which was partially lost in β-LG-LA. There were more binding sites for OA than for LA on β-LG, although the binding constants of the 2 fatty acids were similar, with both acids interacting with the protein though van der Waals and hydrogen bonding interactions. This study could help provide a deeper understanding of the structural basis for formation of antitumor protein-fatty acid complexes.

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