Evaluation of PepT1 transport of food-derived antihypertensive peptides, Ile-Pro-Pro and Leu-Lys-Pro using in vitro, ex vivo and in vivo transport models

Abstract

Publication informationEuropean Journal of Pharmaceutics and Biopharmaceutics, Publisher ElsevierItem record/more information http://hdl.handle.net/10197/8514 an apical buffer pH of 7.4. Gly-Sar reduced the P app across isolated jejunal mucosae and the 32 area under the curve (AUC) in intra-jejunal instillations when the apical/luminal buffer pH 33 was either 7.4 or 6.5. However, the jejunal surface acidic pH was maintained in rat jejunal 34 tissue even when the apical side buffer pH was 7.4 due to the presence of the microclimate 35 which is not present in monolayers. PepT1 expression was confirmed by 36 immunofluorescence on monolayers and brush border of rat jejunal tissue. This data suggest 37 that IPP and LKP are highly permeable and cross small intestinal epithelia in part by the 38 PepT1 transporter, with an additional contribution from the paracellular route. 39 40 41 Publisher's statement þÿ T h i s i s t h e a u t h o r s v e r s i o n o f a w o r k t h a t w a s a c c e p t e d f o r p u b l i c a t i o n i n E u r o p e a n

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

“…The human GIT has many paracellular diffusion pores, also called TJs consisting of zonula occludens‐1, occludin and claudin proteins. Table shows that a variety of DBPs are transported by the energy‐independent paracellular route via TJs (Quirós et al ., ), such as His‐Leu‐Pro‐Leu‐Pro (HLPLP; Quirós et al ., ), Lys‐Val‐Leu‐Pro‐Val‐Pro (KVLPVP; Sun et al ., ), LKP (Gleeson et al ., , ; Xu et al ., ), Arg‐Leu‐Ser‐Phe‐Asn‐Pro (RLSFNP; Guo et al ., ), Arg‐Trp‐Gln (RWQ), Trp‐Gln (WQ; Fernández‐Musoles et al ., ), Ser‐Arg‐Tyr‐Pro‐Ser‐Tyr (SRYPSY), Tyr‐Pro‐Phe‐Pro‐Gly (YPFPG), Tyr‐Pro‐Phe‐Pro‐Gly‐Pro‐Ile (YPFPGPI; Sienkiewicz‐Szłapka et al ., ), Val‐Leu‐Pro‐Val‐Pro (VLPVP; Lei et al ., ) and VPP (Satake et al ., ). However, β‐casein‐f(193–209) cannot be transported via diffusion due to its long length and hydrophobicity (Regazzo et al ., ).…”

“…Peptides are transported via PepT1 coupled with H + . Various DBPs are transported via PepT1 (Table 2), including Ile-Pro-Pro (IPP; Gleeson et al, 2017Gleeson et al, , 2018, Leu-Lys-Pro (LKP; Gleeson et al, 2017Gleeson et al, , 2018Xu et al, 2017), b-Ala-His (Shimizu, 2004) and Tyr-Pro-Ile (Miguel et al, 2008). However, PepT1 cannot transport peptide C (Val-Leu-Pro-Val-Pro-Gln-Lys, VLPVPQK) or BCM-5 (Tyr-Pro-Phe-Pro-Gly, YPFPG; Vij et al, 2016), and its transport capacity is limited to di-and tripeptides only.…”

Isolation of Novel ACE-Inhibitory and Antioxidant Peptides from Quinoa Bran Albumin Assisted with an In Silico Approach: Characterization, In Vivo Antihypertension, and Molecular Docking

“…Until now, many studies have reported the purification, identification, and characterization of antioxidant and ACE inhibition peptides from animal proteins as well as plant and marine proteins. However, the number of studies focused on their in vivo antihypertension, structural bioinformatics, bioavailability, and action mechanism is limited [3,[7][8][9][10][11].…”

“…Quinoa protein is characterized as having a balanced essential amino acid profile and being rich in lysine and methionine, which are the primary deficient amino acids in other cereals like rice, wheat, and maize [13]. The major proteins in quinoa seeds are albumins and globulins, accounting for 35% and 37%, respectively [11]. Recently, much attention has been given to the nutritional value and functional properties of quinoa protein [14,15], and bioactive peptides such as DPP-IV (dipeptidyl-peptidase IV) inhibitory peptides and antioxidant peptides have been identified from quinoa protein isolate and globulin [16][17][18][19].…”

Milk and milk‐derived peptides combat against hypertension and vascular dysfunction: a review

“…Bioavailability of food‐derived components, that is, their absorption from intestine to the systemic circulation is an important issue when examining the physiological effects of nutrients. Ile‐Pro‐Pro, Leu‐Pro‐Pro and Val‐Pro‐Pro have been detected in the circulation after oral administration of dairy products enriched with these peptides both in experimental and human studies (Jauhiainen et al ., ; van der Pijl et al ., ; Kawaguchi et al ., ; Gleeson et al ., ). The levels of the detected tripeptides are low; however, but there were some indications that there was an accumulation of peptides in blood pressure regulating organs.…”