Transepithelial transport of milk derived bioactive peptide VLPVPQK

Vij, Rishika; Reddi, Srinu; Kapila, Suman; Kapila, Rajeev

doi:10.1016/j.foodchem.2015.05.121

Cited by 117 publications

(83 citation statements)

References 35 publications

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“…For example, VPP is rapidly hydrolysed by cytosolic peptidases after being imported into Caco‐2 cells; therefore, intact VPP is mainly transported across monolayers via the paracellular route in vitro (Satake et al ., ). A similar mechanism has been described for transport of bradykinin (RPPGFSPFR; Shimizu et al ., ; Vij et al ., ).…”

Section: Transport Mechanism Of Dbps Across the Intestinal Brush‐bordmentioning

confidence: 97%

“…This is because hydrophobic DBPs must interact with the apical lipid surface via hydrophobic interactions prior to internalization (Shimizu et al ., ). To study the role of transcytosis in transport of DBPs, transcytosis is often inhibited using wortmannin, an inhibitor of phosphoinositide 3‐kinase (Quirós et al ., ; Fernández‐Musoles et al ., ; Vij et al ., ; Wang & Li, ).…”

Section: Transport Mechanism Of Dbps Across the Intestinal Brush‐bordmentioning

confidence: 99%

“…). This pathway is the main transport route for long‐chain DBPs (Regazzo et al ., ), such as bradykinin (Shimizu et al ., ; Vij et al ., ), VLPVPQK and YPFPG (Vij et al ., ), SRYPSY and YPFPGPI (Sienkiewicz‐Szłapka et al ., ) and β‐casein‐f(193–209; Regazzo et al ., ). Notably, DBPs transported via transcytosis are highly hydrophobic.…”

Section: Transport Mechanism Of Dbps Across the Intestinal Brush‐bordmentioning

confidence: 99%

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Current understanding of transport and bioavailability of bioactive peptides derived from dairy proteins: a review

Yan

Zhang

et al. 2018

Int J of Food Sci Tech

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Summary Dairy protein‐derived bioactive peptides (DBPs) have potential benefits for human health. However, their transport mechanisms and bioavailability from intestinal lumen to bloodstream are not well understood. This review summarises current understanding of their transport mechanisms across the intestinal membrane (peptide transport 1, paracellular route, transcytosis and passive transcellular diffusion) and the bioavailability of DBPs in animal and human studies. Some DBPs can escape the degradation of peptidase and reach the bloodstream at concentrations of micromolar range, and keep intact for several minutes to hours. The presences of brush‐border peptidases at the site of absorption and other peptidases in the blood, along with the peptide properties, such as molecular size and weight, stability to proteases, hydrophobicity and charge, determine their bioavailability. Developing novel analytical tools for accurate measurement and study of the transport, metabolism, and bioavailability of DBPs in vivo are expected.

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Section: Transport Mechanism Of Dbps Across the Intestinal Brush‐bordmentioning

confidence: 97%

Section: Transport Mechanism Of Dbps Across the Intestinal Brush‐bordmentioning

confidence: 99%

Section: Transport Mechanism Of Dbps Across the Intestinal Brush‐bordmentioning

confidence: 99%

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Current understanding of transport and bioavailability of bioactive peptides derived from dairy proteins: a review

Yan

Zhang

et al. 2018

Int J of Food Sci Tech

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“…Polypeptides can be absorbed intact except for some forms of small peptides and amino acids, and they can be absorbed via sodium-coupled oligopeptide transporters (SOPT 1 and SOPT2), paracellular passive transport, transcellular passive diffusion and transcytosis [60]. Proteins, similar to polypeptides, can also be absorbed by the paracellular and transcellular pathways.…”

Section: Iron-chelatable Protein Hydrolysatesmentioning

confidence: 99%

Protein Hydrolysates as Promoters of Non-Haem Iron Absorption

Jiang

Huang

2017

Nutrients

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Iron (Fe) is an essential micronutrient for human growth and health. Organic iron is an excellent iron supplement due to its bioavailability. Both amino acids and peptides improve iron bioavailability and absorption and are therefore valuable components of iron supplements. This review focuses on protein hydrolysates as potential promoters of iron absorption. The ability of protein hydrolysates to chelate iron is thought to be a key attribute for the promotion of iron absorption. Iron-chelatable protein hydrolysates are categorized by their absorption forms: amino acids, di- and tri-peptides and polypeptides. Their structural characteristics, including their size and amino acid sequence, as well as the presence of special amino acids, influence their iron chelation abilities and bioavailabilities. Protein hydrolysates promote iron absorption by keeping iron soluble, reducing ferric iron to ferrous iron, and promoting transport across cell membranes into the gut. We also discuss the use and relative merits of protein hydrolysates as iron supplements.

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“…To exert an antihypertensive effect after oral administration, ACE‐inhibitory peptides must remain active after intestinal transport and at least until they reach the cardiovascular system . Several articles have demonstrated that short‐chain ACE‐inhibitory peptides, especially dipeptides and tripeptides, maintained their activity levels after going through the gastrointestinal epithelium process . Satake et al .…”

Section: Introductionmentioning

confidence: 99%