Boc-D-Phe-D-Phe-OH
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Boc-D-Phe-D-Phe-OH

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Category
Others
Catalog number
BAT-000813
Molecular Formula
C23H28N2O5
Molecular Weight
412.5
Storage
Store at 2-8 °C
1. Infinite pleated beta -sheet formed by the beta-hairpin Boc-beta-Phe-beta-Phe-D-Pro-Gly-beta-Phe-beta-Phe-OMe
Isabella Karle, Hosahudya N Gopi, Padmanabhan Balaram Proc Natl Acad Sci U S A. 2002 Apr 16;99(8):5160-4. doi: 10.1073/pnas.022616499. Epub 2002 Mar 5.
A beta-hairpin conformation and extended beta-pleated sheet assembly have been characterized by single crystal x-ray diffraction for the synthetic peptide t-butoxycarbonyl--beta-Phe-beta-Phe-D-Pro-Gly-beta-Phe-beta-Phe-methyl ester [beta-Phe: (S)-beta(3) homophenylalanine]. The centrally located D-Pro-Gly segment nucleates a chain reversal in a type II' beta-turn conformation. Two intramolecular cross-strand hydrogen bonds stabilize the peptide fold. Intermolecular NH...O[double bond]C hydrogen bonds (two on each side of the hairpin) connect the hairpins into an infinitely extended beta-sheet. The beta-residues cause all C[double bond]O groups to point in the same direction, resulting in a "polar" sheet by the unidirectional alignment of NH...O[double bond]C hydrogen bonds. In contrast, beta-sheets formed by alpha-residues have alternating directions for the hydrogen bonds, thus resulting in an "apolar" sheet. The crystallographic parameters for C(53)H(66)N(6)O(9) x CH(3)OH are: space group P2(1), a = 9.854(2) A, b = 10.643(2) A, c = 25.296(4) A, beta = 100.39(2) degrees, Z = 2, agreement factor R(1) = 0.065 for 3,706 data observed >4 sigma(F) and a resolution of 0.90 A.
2. D-Peptide analogues of Boc-Phe-Leu-Phe-Leu-Phe-COOH induce neovascularization via endothelial N-formyl peptide receptor 3
Mohd I Nawaz, et al. Angiogenesis. 2020 Aug;23(3):357-369. doi: 10.1007/s10456-020-09714-0. Epub 2020 Mar 9.
N-formyl peptide receptors (FPRs) are G protein-coupled receptors involved in the recruitment and activation of immune cells in response to pathogen-associated molecular patterns. Three FPRs have been identified in humans (FPR1-FPR3), characterized by different ligand properties, biological function and cellular distribution. Recent findings from our laboratory have shown that the peptide BOC-FLFLF (L-BOC2), related to the FPR antagonist BOC2, acts as an angiogenesis inhibitor by binding to various angiogenic growth factors, including vascular endothelial growth factor-A165 (VEGF). Here we show that the all-D-enantiomer of L-BOC2 (D-BOC2) is devoid of any VEGF antagonist activity. At variance, D-BOC2, as well as the D-FLFLF and succinimidyl (Succ)-D-FLFLF (D-Succ-F3) D-peptide variants, is endowed with a pro-angiogenic potential. In particular, the D-peptide D-Succ-F3 exerts a pro-angiogenic activity in a variety of in vitro assays on human umbilical vein endothelial cells (HUVECs) and in ex vivo and in vivo assays in chick and zebrafish embryos and adult mice. This activity is related to the capacity of D-Succ-F3 to bind FRP3 expressed by HUVECs. Indeed, the effects exerted by D-Succ-F3 on HUVECs are fully suppressed by the G protein-coupled receptor inhibitor pertussis toxin, the FPR2/FPR3 antagonist WRW4 and by an anti-FPR3 antibody. A similar inhibition was observed following WRW4-induced FPR3 desensitization in HUVECs. Finally, D-Succ-F3 prevented the binding of the anti-FPR3 antibody to the cell surface of HUVECs. In conclusion, our data demonstrate that the angiogenic activity of D-Succ-F3 is due to the engagement and activation of FPR3 expressed by endothelial cells, thus shedding a new light on the biological function of this chemoattractant receptor.
3. Development of potent antagonists for formyl peptide receptor 1 based on Boc-Phe-D-Leu-Phe-D-Leu-Phe-OH
Ryo Hayashi, Toshiki Kitajima, Hikaru Mizuguchi, Miki Fujimoto, Aya Yamaguchi, Shuichiro Koga, Yuya Koga, Satoshi Osada, Hiroaki Kodama Bioorg Med Chem. 2014 Aug 1;22(15):3824-8. doi: 10.1016/j.bmc.2014.06.048. Epub 2014 Jul 8.
While stimulation of formyl peptide receptors (FPRs) on the surface of human neutrophils induces several immune responses, under conditions of continuous activation of the receptor by agonists such as formyl-Met-Leu-Phe-OH (fMLP), neutrophil-dependent tissue damage ensues. Thus, FPR antagonists could be anticipated as drugs for FPR-related disease. In this study, Boc-Phe-D-Leu-Phe-D-Leu-Phe-OH (Boc-FlFlF), one of several FPR subtype selective antagonists, was chosen and the positions at the Phe residues were optimized. We found that substitution with unnatural amino acids resulted in an improvement of two orders of magnitude. The most potent antagonist indicated FPR subtype selectivity at 1 μM. In addition to finding a potent antagonist, the structure-activity trends observed in this study should be valuable in designing a new type of FPR subtype selective antagonist.
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