Fmoc-N-Me-Lys(ivDde)-OH
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Fmoc-N-Me-Lys(ivDde)-OH

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Fmoc-N-Me-Lys(ivDde)-OH, an important lysine derivative in peptide synthesis, serves as a fundamental constituent of peptides that target prevalent pathologies such as cancer, diabetes, and cardiovascular disease. Its distinctive nature as a protected amino acid holds significant advantages in research and drug development since it provides peptide molecules with specific, biologically active properties. This feature results in the generation of a diverse range of desirable outcomes for innovative therapeutics and potential cures.

Category
Fmoc-Amino Acids
Catalog number
BAT-008735
CAS number
1173996-67-2
Molecular Formula
C35H44N2O6
Molecular Weight
588.73
Fmoc-N-Me-Lys(ivDde)-OH
IUPAC Name
(2S)-2-[9H-fluoren-9-ylmethoxycarbonyl(methyl)amino]-6-[[1-(2-hydroxy-4,4-dimethyl-6-oxocyclohexen-1-yl)-3-methylbutylidene]amino]hexanoic acid
Synonyms
N2-(((9H-Fluoren-9-yl)methoxy)carbonyl)-N6-(1-(4,4-dimethyl-2,6-dioxocyclohexylidene)-3-methylbutyl)-N2-methyl-L-lysine; L-Lysine, N6-(1-(4,4-dimethyl-2,6-dioxocyclohexylidene)-3-methylbutyl)-N2-((9H-fluoren-9-ylmethoxy)carbonyl)-N2-methyl-
Density
1.176±0.06 g/cm3 (Predicted)
Boiling Point
749.0±60.0°C at 760 mmHg
InChI
InChI=1S/C35H44N2O6/c1-22(2)18-28(32-30(38)19-35(3,4)20-31(32)39)36-17-11-10-16-29(33(40)41)37(5)34(42)43-21-27-25-14-8-6-12-23(25)24-13-7-9-15-26(24)27/h6-9,12-15,22,27,29,38H,10-11,16-21H2,1-5H3,(H,40,41)/t29-/m0/s1
InChI Key
YODHTZQDZIVYMP-LJAQVGFWSA-N
Canonical SMILES
CC(C)CC(=NCCCCC(C(=O)O)N(C)C(=O)OCC1C2=CC=CC=C2C3=CC=CC=C13)C4=C(CC(CC4=O)(C)C)O
1. Activation of cell-penetrating peptide fragments by disulfide formation
Raheleh Tooyserkani, Wojciech Lipiński, Bob Willemsen, Dennis W P M Löwik Amino Acids. 2020 Aug;52(8):1161-1168. doi: 10.1007/s00726-020-02880-x. Epub 2020 Jul 31.
Three cell-penetrating peptides (CPPs), Tat, Pep-3 and penetratin, were split into two parts and each fragment was terminated with a cysteine residue, to allow disulfide bridge formation, as well as a fluorescent label, for visualization and quantitative analysis. After disulfide formation between two complementary CPP fragments, cellular uptake of the resulting conjugates was observed. As confirmed by in vitro experiments, the conjugated peptides showed uptake activity comparable to the native CPP sequences, while the truncated peptides were hardly active. Until now, this split CPP strategy has only been demonstrated for oligo-arginine CPPs, but here we demonstrate that it is also applicable to other cell-penetrating peptides. This wider applicability may help in the design of new activatable cell-penetrating peptides for, e.g., targeted drug delivery.
2. Identification of a novel cell-penetrating peptide targeting human glioblastoma cell lines as a cancer-homing transporter
Moritoshi Higa, et al. Biochem Biophys Res Commun. 2015 Feb 6;457(2):206-12. doi: 10.1016/j.bbrc.2014.12.089. Epub 2015 Jan 3.
Cell-penetrating peptides (CPPs) as a novel biomedical delivery system have been highly anticipated, since they can translocate across biological membranes and are capable of transporting their cargo inside live cells with minimal invasiveness. However, non-selective internalization in various cell types remains a challenge in the clinical application of CPPs, especially in cancer treatment. In this study, we attempted to identify novel cancer-homing CPPs to target glioblastoma multiforme (GBM), which is often refractory and resistant to treatment. We screened for CPPs showing affinity for the human GBM cell line, U87MG, from an mRNA display random peptide library. One of the candidate peptides which amino-acid sequence was obtained from the screening showed selective cell-penetrating activity in U87MG cells. Conjugation of the p16(INK4a) functional peptide to the GBM-selective CPP induced cellular apoptosis and reduced phosphorylated retinoblastoma protein levels. This indicates that the CPP was capable of delivering a therapeutic molecule into U87MG cells inducing apoptosis. These results suggest that the novel CPP identified in this study permeates with high affinity into GBM cells, revealing it to be a promising imaging and therapeutic tool in the treatment of glioblastoma.
3. Effective modification of cell death-inducing intracellular peptides by means of a photo-cleavable peptide array-based screening system
Ikko Kozaki, Kazunori Shimizu, Hiroyuki Honda J Biosci Bioeng. 2017 Aug;124(2):209-214. doi: 10.1016/j.jbiosc.2017.03.013. Epub 2017 Apr 18.
Intracellular functional peptides that play a significant role inside cells have been receiving a lot of attention as regulators of cellular activity. Previously, we proposed a novel screening system for intracellular functional peptides; it combined a photo-cleavable peptide array system with cell-penetrating peptides (CPPs). Various peptides can be delivered into cells and intracellular functions of the peptides can be assayed by means of our system. The aim of the present study was to demonstrate that the proposed screening system can be used for assessing the intracellular activity of peptides. The cell death-inducing peptide (LNLISKLF) identified in a mitochondria-targeting domain (MTD) of the Noxa protein served as an original peptide sequence for screening of peptides with higher activity via modification of the peptide sequence. We obtained 4 peptides with higher activity, in which we substituted serine (S) at the fifth position with phenylalanine (F), valine (V), tryptophan (W), or tyrosine (Y). During analysis of the mechanism of action, the modified peptides induced an increase in intracellular calcium concentration, which was caused by the treatment with the original peptide. Higher capacity for cell death induction by the modified peptides may be caused by increased hydrophobicity or an increased number of aromatic residues. Thus, the present work suggests that the intracellular activity of peptides can be assessed using the proposed screening system. It could be used for identifying intracellular functional peptides with higher activity through comprehensive screening.
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