Anti-inflammatory Effect and Cellular Uptake Mechanism of Peptides from Common Bean (Phaseolus vulga L.) Milk and Yogurts in Caco-2 Mono- and Caco-2/EA.hy926 Co-culture Models

2019 ◽  
Vol 67 (30) ◽  
pp. 8370-8381 ◽  
Author(s):  
Yuhuan Chen ◽  
Hua Zhang ◽  
Lili Mats ◽  
Ronghua Liu ◽  
Zeyuan Deng ◽  
...  
Keyword(s):  
Common Bean ◽  
Cellular Uptake ◽  
Uptake Mechanism ◽  
Culture Models ◽  
Anti Inflammatory ◽  
Cellular Uptake Mechanism ◽  
Inflammatory Effect

Cellular Uptake Mechanism of Molecular Umbrella

2009 ◽  
Vol 20 (12) ◽  
pp. 2311-2316 ◽  
Author(s):  
Dongtao Ge ◽  
Dewang Wu ◽  
Zuyong Wang ◽  
Wei Shi ◽  
Ting Wu ◽  
...  
Keyword(s):  
Cellular Uptake ◽  
Uptake Mechanism ◽  
Cellular Uptake Mechanism

scholarly journals Cellular Uptake Mechanism of Cationic Branched Polypeptides with Poly[l-Lys] Backbone

2017 ◽  
Vol 19 (4) ◽  
pp. 246-254 ◽  
Author(s):  
Rita Szabó ◽  
Mónika Sebestyén ◽  
György Kóczán ◽  
Ádám Orosz ◽  
Gábor Mező ◽  
...  
Keyword(s):  
Cellular Uptake ◽  
Uptake Mechanism ◽  
Cellular Uptake Mechanism

scholarly journals C-Terminal Amination of a Cationic Anti-Inflammatory Peptide Improves Bioavailability and Inhibitory Activity Against LPS-Induced Inflammation

2021 ◽  
Vol 11 ◽  
Author(s):  
Lulu Zhang ◽  
Xubiao Wei ◽  
Rijun Zhang ◽  
Matthew Koci ◽  
Dayong Si ◽  
...  
Keyword(s):  
Cellular Uptake ◽  
Cell Uptake ◽  
Inflammatory Activity ◽  
Myeloid Differentiation ◽  
Toll Like Receptor 4 ◽  
Native Peptides ◽  
Anti Inflammatory ◽  
Myeloid Differentiation Factor ◽  
Inflammatory Effect ◽  
Lps Binding

Lipopolysaccharide (LPS) has been implicated as a major cause of inflammation and an uncontrolled LPS response increases the risk of localized inflammation and sepsis. While some native peptides are helpful in the treatment of LPS-induced inflammation, the use of these peptides is limited due to their potential cytotoxicity and poor anti-inflammatory activity. Hybridization is an effective approach for overcoming this problem. In this study, a novel hybrid anti-inflammatory peptide that combines the active center of Cathelicidin 2 (CATH2) with thymopentin (TP5) was designed [CTP, CATH2 (1–13)-TP5]. CTP was found to have higher anti-inflammatory effects than its parental peptides through directly LPS neutralization. However, CTP scarcely inhibited the attachment of LPS to cell membranes or suppressed an established LPS-induced inflammation due to poor cellular uptake. The C-terminal amine modification of CTP (CTP-NH2) was then designed based on the hypothesis that C-terminal amidation can enhance the cell uptake by increasing the hydrophobicity of the peptide. Compared with CTP, CTP-NH2 showed enhanced anti-inflammatory activity and lower cytotoxicity. CTP-NH2 not only has strong LPS neutralizing activity, but also can significantly inhibit the LPS attachment and the intracellular inflammatory response. The intracellular anti-inflammatory effect of CTP-NH2 was associated with blocking of LPS binding to the Toll-like receptor 4-myeloid differentiation factor 2 complex and inhibiting the nuclear factor-kappa B pathway. In addition, the anti-inflammatory effect of CTP-NH2 was confirmed using a murine LPS-induced sepsis model. Collectively, these findings suggest that CTP-NH2 could be developed into a novel anti-inflammatory drug. This successful modification provides a design strategy to improve the cellular uptake and anti-inflammatory activity of peptide agents.

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