Inhibition of Angiotensin-converting Enzyme by Synthetic Peptides of Human β-Casein

Bioactive peptides released from in vitro digestion of human milk with or without pasteurization

“…This region provides a PEPi peptide, previously investigated as an anticancer peptide (residues 122-131) (23), an ACEi peptide (residues 122-129) (17) and another PEPi peptide, studied in the context of learning and memory processes (residues 125-130) (19). While their roles in vivo have scarcely been investigated, all these peptides would also be precursors for a potent ACEi peptide of residues 125-129 (HLPLP) (22).…”

“…The most abundant peptides are derived from β-CN, reflecting its high susceptibility to plasmin-mediated proteolysis as well as the high content of this casein subunit in HM (14,16). Focusing on bioactive peptides in undigested HM, as shown in Table 1 (14,15,(17)(18)(19)(20)(21)(22)(23)(24)(25)(26)(27)(28)(29)(30), two caseinophosphopeptide homologues, a possible opioid peptide or propeptide, and an antibacterial peptide were identified.…”

In silico analysis and antihypertensive effect of ACE-inhibitory peptides from smooth-hound viscera protein hydrolysate: Enzyme-peptide interaction study using molecular docking simulation

“…Thus, VVPFEGAV could be ACE inhibitor. Moreover, the peptide PLPKREE contained the ACE inhibitor tri-peptide PLP (IC50 = 430 µM) [52] and the anti-thrombotic tetra-peptide KREE [53]. DSFEGLQQ shows the sequence LQQ in its C-terminus, which is an ACE-inhibitor peptide with an IC50 value of 100 µM [54].…”

Synthesis of the bradykinin B1 antagonist [desArg10]HOE 140 on 2-chlorotrityl resin

“…The problem of DKP formation during Fmoc removal with piperidine from a resin-linked dipeptide, with consequent loss of the peptide, is well documented in the literature [10][11][12][13][14]. The synthesis of the B1 antagonist [desArg~°]HOE 140, the sequence of which is characterized by the C-terminal D-Tic-Oic-OH dipeptide, is predicted to be particularly prone to this problem, due to the imino acidic structure of both these residues and the D-configuration of the second one.…”

“…This well-known side reaction consists of the intramolecular aminolysis of the C-kerminal dipeptide, with consequent loss of the peptidic chain from the resin [3]. The reaction, which is particularly rapid when the dipep- tide sequence includes glycine, proline, N~-methyl or D-amino acid residues, has been widely discussed in the literature, particularly for peptides containing C-terminal proline residue(s), referring to both the Boc strategy, with a benzyl ester resin linkage [4][5][6][7][8][9], and the Fmoc strategy, with a palkoxybenzyl alcohol resin linkage [10][11][12][13][14]. The most straightforward solution to avoid this side reaction consists in the coupling of a preformed dipeptide onto the resin-linked C-terminal residue, in order to overcome the dipeptide stage [10,13].…”