κ-casein Inhibitors
Chemical inhibitors of κ-casein can lead to the functional disruption of this protein through various molecular interactions. Benzyl isothiocyanate can react with cysteine residues in κ-casein, forming thioureas, which may lead to structural alterations that compromise its ability to stabilize casein micelles. Similarly, Epigallocatechin gallate (EGCG) is capable of binding to κ-casein and inducing conformational changes that inhibit its micelle-stabilizing functions. Dithiothreitol (DTT) can cleave disulfide bonds within κ-casein, which are critical for maintaining its three-dimensional structure, thereby inhibiting its interaction with other casein molecules and its role in maintaining micelle structure. Chlorogenic acid and tannic acid both have the ability to non-covalently bind to hydrophobic regions or form protein complexes, respectively, which potentially alters κ-casein conformation and reduces its functional capacity in micelle stabilization.
Further, ellagic acid can bind to κ-casein and disrupt its structure, thus preventing the protein from effectively contributing to casein micelle stability. Curcumin is known to interact with κ-casein, inducing structural changes that inhibit its function in micelle formation. Genistein's protein-binding properties allow it to bind to κ-casein, potentially altering the protein's conformation and impairing its role in micelle stabilization. Caffeic acid can also bind to κ-casein, potentially altering its structural integrity and negatively impacting micelle formation. Capsaicin, with its lipophilic character, can intercalate into κ-casein's structure, disrupting necessary protein interactions for micelle stability. Quercetin and naringenin can both bind to κ-casein, leading to conformational changes that reduce the protein's effectiveness in stabilizing casein micelles. These chemical interactions with κ-casein underscore the diverse mechanisms through which the protein's functional role in micelle stability can be inhibited.
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| Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
|---|---|---|---|---|---|---|
Benzyl isothiocyanate | 622-78-6 | sc-204641 sc-204641A | 5 g 25 g | $47.00 $156.00 | 1 | |
Benzyl isothiocyanate can inhibit κ-casein by reacting with cysteine residues in the protein, potentially altering its structure and function through the formation of thioureas, which could disrupt the micelle-stabilizing role of κ-casein in milk. | ||||||
(−)-Epigallocatechin Gallate | 989-51-5 | sc-200802 sc-200802A sc-200802B sc-200802C sc-200802D sc-200802E | 10 mg 50 mg 100 mg 500 mg 1 g 10 g | $43.00 $73.00 $126.00 $243.00 $530.00 $1259.00 | 11 | |
Epigallocatechin gallate (EGCG) is known to bind proteins and may inhibit κ-casein by directly interacting with its amino acid residues, leading to conformational changes that inhibit the protein's ability to stabilize casein micelles. | ||||||
Chlorogenic Acid | 327-97-9 | sc-204683 sc-204683A | 500 mg 1 g | $47.00 $69.00 | 1 | |
Chlorogenic acid may inhibit κ-casein by non-covalently binding to its hydrophobic regions, potentially altering the protein's conformation and reducing its ability to stabilize casein micelles. | ||||||
Gallotannin | 1401-55-4 | sc-202619 sc-202619A sc-202619B sc-202619C sc-202619D sc-202619E sc-202619F | 1 g 10 g 100 g 250 g 1 kg 2.5 kg 5 kg | $26.00 $37.00 $67.00 $78.00 $234.00 $536.00 $983.00 | 12 | |
Tannic acid could inhibit κ-casein by forming complexes with the protein through non-specific interactions, which may lead to precipitation or conformational changes that inhibit its function in the milk micelle system. | ||||||
Ellagic Acid, Dihydrate | 476-66-4 | sc-202598 sc-202598A sc-202598B sc-202598C | 500 mg 5 g 25 g 100 g | $58.00 $95.00 $245.00 $727.00 | 8 | |
Ellagic acid has the potential to inhibit κ-casein by binding to its polypeptide chain and disrupting its structure, which can prevent the protein from contributing to the stabilization of casein micelles. | ||||||
Curcumin | 458-37-7 | sc-200509 sc-200509A sc-200509B sc-200509C sc-200509D sc-200509F sc-200509E | 1 g 5 g 25 g 100 g 250 g 1 kg 2.5 kg | $37.00 $69.00 $109.00 $218.00 $239.00 $879.00 $1968.00 | 47 | |
Curcumin can inhibit κ-casein function by directly interacting with the protein and inducing conformational changes, which may reduce the protein's ability to interact with other casein molecules within the micelle structure. | ||||||
Genistein | 446-72-0 | sc-3515 sc-3515A sc-3515B sc-3515C sc-3515D sc-3515E sc-3515F | 100 mg 500 mg 1 g 5 g 10 g 25 g 100 g | $45.00 $164.00 $200.00 $402.00 $575.00 $981.00 $2031.00 | 46 | |
Genistein may inhibit κ-casein by binding to its surface, potentially altering the protein's conformation and impairing its micelle-stabilizing role due to the compound's known protein-binding properties. | ||||||
Caffeic Acid | 331-39-5 | sc-200499 sc-200499A | 1 g 5 g | $32.00 $62.00 | 1 | |
Caffeic acid can inhibit κ-casein by binding to the protein and potentially altering its structural integrity, which may negatively impact its role in micelle formation and maintenance. | ||||||
Capsaicin | 404-86-4 | sc-3577 sc-3577C sc-3577D sc-3577A | 50 mg 250 mg 500 mg 1 g | $96.00 $160.00 $240.00 $405.00 | 26 | |
Capsaicin could inhibit κ-casein by intercalating into the protein structure and disrupting interactions necessary for its function in micelle stability, due to its lipophilic nature and ability to interact with proteins. | ||||||
Quercetin | 117-39-5 | sc-206089 sc-206089A sc-206089E sc-206089C sc-206089D sc-206089B | 100 mg 500 mg 100 g 250 g 1 kg 25 g | $11.00 $17.00 $110.00 $250.00 $936.00 $50.00 | 33 | |
Quercetin may inhibit κ-casein by binding to the protein, potentially causing conformational changes that reduce its effectiveness in stabilizing casein micelles. | ||||||