48065-82-3

Basic information

• Product Name: Nε-acryloyl-L-lysin
• Synonyms: Nε-acryloyl-L-lysin;N6-(1-Oxo-2-propen-1-yl)-L-lysine;N-epsilon-Acryloyl L-Lysine;NSC 288650;2-amino-6-(prop-2-enoylamino)hexanoic acid;L-Lysine, N6-(1-oxo-2-propen-1-yl)-;(S)-6-Acrylamido-2-aminohexanoic acid
• CAS NO: 48065-82-3
• Molecular Formula: C9H16N2O3
• Molecular Weight: 200.23494
• Mol File: 48065-82-3.mol
• Article Data: 13

Chemical Properties

• Boiling Point: 453.9°Cat760mmHg
• Flash Point: 228.3°C
• Appearance: /
• Density: 1.132g/cm³
• Vapor Pressure: 1.67E-09mmHg at 25°C
• Refractive Index: 1.501
• PKA: 2.53±0.24(Predicted)
• CAS DataBase Reference: Nε-acryloyl-L-lysin(CAS DataBase Reference)
• NIST Chemistry Reference: Nε-acryloyl-L-lysin(48065-82-3)
• EPA Substance Registry System: Nε-acryloyl-L-lysin(48065-82-3)

Safety Data

• Hazardous Substances Data: 48065-82-3(Hazardous Substances Data)

Usage

General Description

Nε-acryloyl-L-lysine is an amino acid derivative that is commonly used in the development of advanced materials and biomaterials. Nε-acryloyl-L-lysin contains an acryloyl group, which makes it suitable for incorporation into polymers and hydrogels through a variety of chemical reactions. Nε-acryloyl-L-lysine has been utilized in the synthesis of biocompatible materials for tissue engineering, drug delivery, and other medical applications, due to its ability to promote cell adhesion and proliferation. Its reactive nature also allows for the modification of surfaces and the development of functional coatings with tailored properties. Overall, Nε-acryloyl-L-lysine plays a crucial role in the creation of innovative materials with potential uses in biotechnology and biomedicine.

InChI:InChI=1/C9H16N2O3/c1-2-8(12)11-6-4-3-5-7(10)9(13)14/h2,7H,1,3-6,10H2,(H,11,12)(H,13,14)

Upstream product

• 2051-76-5 acrylic acid anhydride 
• 850416-32-9 (2S)-2-{[(tert-butoxy)carbonyl]amino}-6-(prop-2-enamido)hexanoic acid 
• 13734-28-6 Boc-Lys-OH 
• 657-27-2 L-Lysine hydrochloride 
• 814-68-6 acryloyl chloride 
• 38862-24-7 N-(acryloyloxy)succinimide 
• 26124-78-7 (S)-α-lysine hydrochloride 
• 56-87-1 L-lysine 

Relevant articles and documents

A genetically encoded aza-michael acceptor for covalent cross-linking of protein-receptor complexes

Selective covalent bond formation at a protein-protein interface potentially can be achieved by genetically introducing into a protein an appropriately tuned electrophilic unnatural amino acid that reacts with a native nucleophilic residue in its cognate receptor upon complex formation. We have evolved orthogonal aminoacyl-tRNA synthetase/tRNACUA pairs that genetically encode three aza-Michael acceptor amino acids, Nε- acryloyl-(S)-lysine (AcrK, 1), p-acrylamido-(S)-phenylalanine (AcrF, 2), and p-vinylsulfonamido-(S)-phenylalanine (VSF, 3), in response to the amber stop codon in Escherichia coli. Using an αErbB2 Fab-ErbB2 antibody-receptor pair as an example, we demonstrate covalent bond formation between an αErbB2-VSF mutant and a specific surface lysine ε-amino group of ErbB2, leading to near quantitative cross-linking to either purified ErbB2 in vitro or to native cellular ErbB2 at physiological pH. This efficient biocompatible reaction may be useful for creating novel cell biological probes, diagnostics, or therapeutics that selectively and irreversibly bind a target protein in vitro or in living cells.

Strength-tunable printing of xanthan gum hydrogel: Via enzymatic polymerization and amide bioconjugation

Amide bioconjugation and interfacial enzyme polymerization are designed to provide a general strategy for regulating the mechanical strength (storage modulus from 3 kPa to 100 kPa) of printable hydrogel inks.

A GENETICALLY ENCODED, PHAGE-DISPLAYED CYCLIC PEPTIDE LIBRARY AND METHODS OF MAKING THE SAME

Embodiments of the present disclosure pertain to methods of selecting cyclic peptides that bind to a target by transforming a phage display library with a plurality of nucleic acids into bacterial host cells, where the nucleic acids include phage coat protein genes with a combinatorial region that encodes at least one cysteine and at least one non-canonical amino acid. The transformation results in the production of phage particles with phage coat proteins where the cysteine and the non-canonical amino acid couple to one another to form a cyclic peptide library. Phage particles are then screened against the desired target to select bound cyclic peptides. Amino acid sequences of the selected cyclic peptides are then identified. Additional embodiments pertain to methods of constructing a phage display library that encodes the cyclic peptides. Further embodiments of the present disclosure pertain to the produced cyclic peptides, phage display libraries and phage particles.

A Genetically Encoded, Phage-Displayed Cyclic-Peptide Library

Superior to linear peptides in biological activities, cyclic peptides are considered to have great potential as therapeutic agents. To identify cyclic-peptide ligands for therapeutic targets, phage-displayed peptide libraries in which cyclization is achieved by the covalent conjugation of cysteines have been widely used. To resolve drawbacks related to cysteine conjugation, we have invented a phage-display technique in which its displayed peptides are cyclized through a proximity-driven Michael addition reaction between a cysteine and an amber-codon-encoded N?-acryloyl-lysine (AcrK). Using a randomized 6-mer library in which peptides were cyclized at two ends through a cysteine–AcrK linker, we demonstrated the successful selection of potent ligands for TEV protease and HDAC8. All selected cyclic peptide ligands showed 4- to 6-fold stronger affinity to their protein targets than their linear counterparts. We believe this approach will find broad applications in drug discovery.