Name: Fmoc-Lys(Pal-Glu-OtBu)-OH
Brand: BOC Sciences
Rating: 5 (1 reviews)

Synonyms

(2S)-6-[(4S)-5-(tert-Butoxy)-4-hexadecanamido-5-oxopentanamido]-2-({[(9H-fluoren-9-yl)methoxy]carbonyl}amino)hexanoic acid; Fmoc-L-Lys(Pal-L-Glu-OtBu)-OH; N-alpha-(9-Fluorenylmethyloxycarbonyl)-N-epsilon-(N-alpha'-palmitoyl-L-glutamic-acid alpha'-t-butyl ester)-L-lysine; Fmoc-L-Lys(Palm-L-Glu-OtBu); Fmoc-L-Lys(Pal-L-Glu-OtBu); N2-(((9H-Fluoren-9-yl)methoxy)carbonyl)-N6-((S)-5-(tert-butoxy)-5-oxo-4-palmitamidopentanoyl)-L-lysine; palmitoyl-L-Glu(1)-OtBu.Fmoc-L-Lys(1)-OH; (S)-2-((((9H-Fluoren-9-yl)methoxy)carbonyl)amino)-6-((S)-5-(tert-butoxy)-5-oxo-4-palmitamidopentanamido)hexanoic acid; Fmoc-L-Lys(Palmitoyl-L-Glu-OtBu)-OH; Fmoc-Lys(Palm-L-Glu-OtBu)-OH; Fmoc-L-Lys(Palm-L-Glu-OtBu)-OH; N2-[(9H-Fluoren-9-ylmethoxy)carbonyl]-N6-[N-(1-oxohexadecyl)-L-γ-glutamyl]-L-lysine 1'-(1,1-dimethylethyl) ester

IUPAC Name

(2S)-2-(9H-fluoren-9-ylmethoxycarbonylamino)-6-[[(4S)-4-(hexadecanoylamino)-5-[(2-methylpropan-2-yl)oxy]-5-oxopentanoyl]amino]hexanoic acid

Canonical SMILES

CCCCCCCCCCCCCCCC(=O)NC(CCC(=O)NCCCCC(C(=O)O)NC(=O)OCC1C2=CC=CC=C2C3=CC=CC=C13)C(=O)OC(C)(C)C

InChI

InChI=1S/C46H69N3O8/c1-5-6-7-8-9-10-11-12-13-14-15-16-17-29-42(51)48-40(44(54)57-46(2,3)4)30-31-41(50)47-32-23-22-28-39(43(52)53)49-45(55)56-33-38-36-26-20-18-24-34(36)35-25-19-21-27-37(35)38/h18-21,24-27,38-40H,5-17,22-23,28-33H2,1-4H3,(H,47,50)(H,48,51)(H,49,55)(H,52,53)/t39-,40-/m0/s1

InChIKey

LQQXBYSAGYOQJW-ZAQUEYBZSA-N

Sequence

Fmoc-Lys(Pal-Glu-OtBu)

Density

1.099±0.06 g/cm3

Appearance

White to off-white solid

Storage

Store at 2-8 °C

Boiling Point

944.2±65.0 °C at 760 mmHg

Fmoc-Lys(Pal-Glu-OtBu)-OH is a modified lysine derivative widely used in peptide synthesis, particularly for creating lipidated peptides. The Fmoc (9-fluorenylmethyloxycarbonyl) group serves as a protective group for the amino terminus, facilitating controlled sequential assembly in solid-phase peptide synthesis (SPPS). This enables the incorporation of the compound into complex peptide sequences with high precision, making it a versatile building block for the synthesis of bioactive peptides and functionalized biomolecules.

The Pal-Glu-OtBu modification is the defining feature of Fmoc-Lys(Pal-Glu-OtBu)-OH. The palmitoyl (Pal) group introduces lipid-like properties into the peptide, enhancing its hydrophobicity and membrane affinity. This is particularly important in the development of lipopeptides, which are widely studied for their applications in vaccine development, drug delivery systems, and antimicrobial therapies. The Glu-OtBu (tert-butoxy-protected glutamic acid) moiety provides additional versatility by protecting the carboxyl group, ensuring stability during peptide synthesis and allowing for selective deprotection when needed.

One key application of Fmoc-Lys(Pal-Glu-OtBu)-OH is in the design of cell-penetrating peptides (CPPs). The incorporation of a palmitoyl group enhances the ability of peptides to interact with and traverse cellular membranes, making them suitable for delivering therapeutic agents, such as small molecules, nucleic acids, or proteins, into cells. This functionality is critical for developing peptide-based drug delivery systems and improving the bioavailability of therapeutic compounds.

Fmoc-Lys(Pal-Glu-OtBu)-OH is also valuable in the synthesis of self-assembling peptide systems. The hydrophobicity introduced by the palmitoyl group promotes peptide aggregation and the formation of nanostructures, such as micelles or hydrogels. These systems have applications in tissue engineering, drug delivery, and as scaffolds for regenerative medicine. By incorporating this compound, researchers can design peptide-based materials with tunable properties, combining structural integrity with bioactivity.

In addition, Fmoc-Lys(Pal-Glu-OtBu)-OH is used in the development of vaccine adjuvants and immunomodulatory peptides. The lipidation enhances antigen presentation and immune activation, making it a critical component in synthetic vaccine design. This property is especially useful in creating lipopeptide-based formulations that boost immunogenicity while maintaining biocompatibility.

1. Solid-Phase Synthesis of Fluorescent Probes for Plasma Membrane Labelling

Shuo Zhang, Annamaria Lilienkampf, Mark Bradley Molecules. 2021 Jan 12;26(2):354. doi: 10.3390/molecules26020354.

The cellular plasma membrane plays a fundamental role in biological processes, including cell growth, signaling and transport. The labelling of the plasma membrane with targeted fluorescent probes offers a convenient and non-invasive way to image the morphological changes and dynamics of a membrane in real-time and, despite many examples of fluorescent plasma membrane probes, a "universal targeting/anchoring moiety" is still required. In this study, a small number of stearic acid-based probes labelled with 6-carboxyfluorescein was designed and fabricated via solid-phase synthesis in which variations in both charge and hydrophobicity were explored. To ease the synthesis process, a gram-scale synthesis of the Fmoc-Lys(6-carboxyfluoresein diacetate)-OH building block was developed, allowing the discovery of optimal probes that carried a positively charged amino group and a stearic acid tail that exhibited intense plasma membrane brightness and robust retention.

2. Enhancing the antibacterial effect of chitosan to combat orthopaedic implant-associated infections

Dien Puji Rahayu, Arianna De Mori, Rahmi Yusuf, Roger Draheim, Aikaterini Lalatsa, Marta Roldo Carbohydr Polym. 2022 Aug 1;289:119385. doi: 10.1016/j.carbpol.2022.119385. Epub 2022 Mar 28.

The development of antibacterial resistance imposes the development of novel materials to relieve the burden of infection. Chitosan, a material of natural and sustainable origin, possesses ideal characteristics to translate into a novel biomaterial with antibacterial properties, as it already has these properties and it allows easy and scalable chemical modification to enhance its activity. The aim of the present work was that of producing low molecular weight chitosans that have higher solubility and can remain protonated at physiological pH, thus enhancing the antimicrobial action. This was achieved by reacting acid hydrolysed low molecular weight chitosan with 2-bromoethyleneamine hydrobromide or Fmoc-Lys(Fmoc)-OH to elicit N-(2-ethylamino)-chitosan and N-2(2,6-diaminohexanamide)-chitosan polymers. The latter derivative, CS3H Lys, that was synthesised for the first time, showed superior efficacy against Staphylococcus aureus, supporting further studies for its inclusion in implant coating materials to tackle the burden of orthopaedic implant-associated infections.

3. The use of Fmoc-Lys(Pac)-OH and penicillin G acylase in the preparation of novel semisynthetic insulin analogs

Lenka Záková, Daniel Zyka, Jan Jezek, Ivona Hanclová, Miloslav Sanda, Andrzej M Brzozowski, Jirí Jirácek J Pept Sci. 2007 May;13(5):334-41. doi: 10.1002/psc.847.

In this paper, we present the detailed synthetic protocol and characterization of Fmoc-Lys(Pac)-OH, its use for the preparation of octapeptides H-Gly-Phe-Tyr-N-MePhe-Thr-Lys(Pac)-Pro-Thr-OH and H-Gly-Phe-Phe-His-Thr-Pro-Lys(Pac)-Thr-OH by solid-phase synthesis, trypsin-catalyzed condensation of these octapeptides with desoctapeptide(B23-B30)-insulin, and penicillin G acylase catalyzed cleavage of phenylacetyl (Pac) group from Nepsilon-amino group of lysine to give novel insulin analogs [TyrB25, N-MePheB26,LysB28,ProB29]-insulin and [HisB26]-insulin. These new analogs display 4 and 78% binding affinity respectively to insulin receptor in rat adipose membranes.