Interactions of α-Lactalbumin with Fatty Acids and Spin Label Analogs

Donkey milk could be considered a good and safer alternative, compared to other types of milk, for infants affected by cow's milk protein allergy, when breastfeeding is not possible. Interestingly, donkey milk has low allergenicity, mainly due to the low total casein amount, and the content of some whey proteins that act as bioactive peptides. The amount of lysozyme, an antibacterial agent, is 1.0 g/L, similar to human milk. Lactoferrin content is 0.08 g/L, with this protein being involved in the regulation of iron homoeostasis, anti-microbial and anti-viral functions, and protection against cancer development. Lactoperoxidase, another protein with antibacterial function, is present in donkey milk, but in very low quantities (0.11 mg/L). β-lactoglobulin content in donkey milk is 3.75 g/L-this protein is able to bind and transport several hydrophobic molecules. Donkey milk's α-lactalbumin concentration is 1.8 g/L, very close to that of human milk. α-lactalbumin shows antiviral, antitumor, and anti-stress properties. Therefore, donkey milk can be considered as a set of nutraceuticals properties and a beverage suitable, not only for the growing infants, but for all ages, especially for convalescents and for the elderly.

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“…Finally, it was demonstrated that native α-La possesses several classes of fatty acid binding site [52].…”

Section: α-Lactalbuminmentioning

confidence: 99%

Role of Proteins and of Some Bioactive Peptides on the Nutritional Quality of Donkey Milk and Their Impact on Human Health

et al. 2017

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“…The very small variation in the transition temperature or the calorimetric enthalpy of the protein unfolding in presence of high concentrations of lipid supports that at the physiological pH (7.4), a-lactalbumin adsorbs only to the outer surface of the phospholipid vesicles by electrostatic attraction [31]. It also supports that calcium-enriched a-lactalbumin has a low affinity towards association to model membranes [17]. The average value of the ratio of van't Hoff to calorimetric enthalpy is 0.99F0.07, indicating that the thermal unfolding of protein in presence of DPPC is reversible and two state.…”

Section: Differential Scanning Calorimetric Studies On Thermal Transimentioning

confidence: 65%

“…However, significant association between alactalbumin and fatty acid has not been observed [16]. a-Lactalbumin has been found to be associated with milk fat globule membranes, suggesting a possible role for this protein in fat digestion or transport [17]. a-Lactalbumin is one of the two components of lactose synthase, which catalyzes the final step of lactose biosynthesis in lactating mammary gland.…”

Section: Introductionmentioning

confidence: 97%

Thermodynamics of α-lactalbumin–dl-α-dipalmitoylphosphatidylcholine interactions and effect of the antioxidant nicotinamide on these interactions

Kundu

Kishore

2005

Biophysical Chemistry

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“…Alpha-lactalbumin possesses several fatty acid binding sites, and has been shown to bind stearic acid, palmitic acid and oleic acid spin-labelled fatty acid analogs [6,41]. The release of the Ca 2+ ion and subsequent unfolding of the protein triggers -LA to achieve a new fatty acid binding profile, with a higher affinity for cis-unsaturated fatty acids than for the corresponding trans conformations.…”

Section: Fatty Acid Binding Profile Of α-Lamentioning

confidence: 99%

“…Site-specific labeling of HAMLET and HAMLET-like complexes with aminooxy-Alexa Fluor 488 or biotin molecules has also been used [52]. It has previously been described that -LA interacts with cell membranes and lipid bilayers, as well as fatty acids [41,[70][71][72][73][74]. In addition, it has been observed that -LA is able to rapidly insert itself into the lipid bilayer at pH 2 [75].…”

Section: Cellular Trafficking Of Hamletmentioning

confidence: 99%