1428330-91-9

Basic information

• Product Name: N-ε-propargyloxycarbonyl-L-lysine hydrochloride
• Synonyms: N-ε-propargyloxycarbonyl-L-lysine hydrochloride;N6-[(2-Propyn-1-yloxy)carbonyl]-L-lysine HCl;(S)-2-amino-6-(((prop-2-yn-1-yloxy)carbonyl)amino)hexanoic acid hydrochloride(WXC08619S1);(S)-2-amino-6-((prop-2-ynyloxy)carbonylamino)hexanoic acid hydrochloride;(S)-2-amino-6-(((prop-2-yn-1-yloxy)carbonyl)amino)hexanoicacidhydrochloride
• CAS NO: 1428330-91-9
• Molecular Formula: C10H16N2O4
• Molecular Weight: 228.24504
• Mol File: 1428330-91-9.mol

Chemical Properties

• Appearance: /
• CAS DataBase Reference: N-ε-propargyloxycarbonyl-L-lysine hydrochloride(CAS DataBase Reference)
• NIST Chemistry Reference: N-ε-propargyloxycarbonyl-L-lysine hydrochloride(1428330-91-9)
• EPA Substance Registry System: N-ε-propargyloxycarbonyl-L-lysine hydrochloride(1428330-91-9)

Safety Data

• Hazardous Substances Data: 1428330-91-9(Hazardous Substances Data)

Usage

Uses

Used in Bioconjugation and Protein Modification:
N-ε-propargyloxycarbonyl-L-lysine hydrochloride is used as a bioconjugation agent for the selective labeling of proteins and peptides. Its propargylamine functional group allows for the formation of stable covalent bonds with biomolecules, facilitating the development of novel bioconjugates with enhanced properties and functionalities.
Used in Synthesis of Novel Biomolecules and Bioconjugates:
In the field of chemical biology, N-ε-propargyloxycarbonyl-L-lysine hydrochloride is utilized as a key building block in the synthesis of innovative biomolecules and bioconjugates. Its unique reactivity and versatility enable the creation of new chemical tools and therapeutic agents with improved targeting, delivery, and efficacy.
Used in Targeted Drug Delivery Systems:
N-ε-propargyloxycarbonyl-L-lysine hydrochloride is employed as a component in the development of targeted drug delivery systems. Its ability to selectively label proteins and peptides allows for the precise attachment of therapeutic agents to specific biological targets, enhancing the efficacy and reducing the side effects of treatments.
Used in Molecular Imaging Agents:
In molecular imaging, N-ε-propargyloxycarbonyl-L-lysine hydrochloride is used as a component in the design of imaging agents. Its selective labeling capabilities enable the attachment of imaging moieties to specific biomolecules, allowing for the visualization and tracking of biological processes and disease progression with high specificity and sensitivity.
Overall, N-ε-propargyloxycarbonyl-L-lysine hydrochloride's unique properties and reactivity make it a valuable asset in various industries, including pharmaceuticals, chemical biology, and molecular imaging, for the development of innovative solutions and therapeutic agents.

Upstream product

• 1202704-91-3 N²-(tert-butoxycarbonylamino)-N⁶-[(prop-2-yn-1-yloxy)carbonyl]-L-lysine 
• 1167421-24-0 (S)-15-azido-2,2-dimethyl-4,12-dioxo-3,13-dioxa-5,11-diazapentadecane-6-carboxylic acis 
• 1167421-25-1 (2S)-2-amino-6-{[(2-azidoethoxy)carbonyl]amino}hexanoic acid 
• 1364218-52-9 N-Boc-N^ε-((2-bromoethoxy)carbonyl)lysine 
• 13734-28-6 Boc-Lys-OH 

Relevant articles and documents

Click strategies for single-molecule protein fluorescence

Single-molecule methods have matured into central tools for studies in biology. Foerster resonance energy transfer (FRET) techniques, in particular, have been widely applied to study biomolecular structure and dynamics. The major bottleneck for a facile and general application of these studies arises from the need to label biological samples site-specifically with suitable fluorescent dyes. In this work, we present an optimized strategy combining click chemistry and the genetic encoding of unnatural amino acids (UAAs) to overcome this limitation for proteins. We performed a systematic study with a variety of clickable UAAs and explored their potential for high-resolution single-molecule FRET (smFRET). We determined all parameters that are essential for successful single-molecule studies, such as accessibility of the probes, expression yield of proteins, and quantitative labeling. Our multiparameter fluorescence analysis allowed us to gain new insights into the effects and photophysical properties of fluorescent dyes linked to various UAAs for smFRET measurements. This led us to determine that, from the extended tool set that we now present, genetically encoding propargyllysine has major advantages for state-of-the-art measurements compared to other UAAs. Using this optimized system, we present a biocompatible one-step dual-labeling strategy of the regulatory protein RanBP3 with full labeling position freedom. Our technique allowed us then to determine that the region encompassing two FxFG repeat sequences adopts a disordered but collapsed state. RanBP3 serves here as a prototypical protein that, due to its multiple cysteines, size, and partially disordered structure, is not readily accessible to any of the typical structure determination techniques such as smFRET, NMR, and X-ray crystallography.

A facile system for genetic incorporation of two different noncanonical amino acids into one protein in Escherichia coli

Two's company: Using a wild-type or evolved PylRS-pylTUUA pair to suppress ochre mutation and an evolved MjTyrRSMjtRNACUA Tyr pair to suppress amber mutation, two different noncanonical amino acids (NAAs) have been concomitantly incorporated into one protein in E. coli with high efficiency (see picture, with NAAs 1-4; GFP = green-fluorescent protein). "Chemical equation presented"