98891-36-2

Basic information

• Product Name: (S)-2-AMINOHEX-5-YNOIC ACID
• Synonyms: (S)-2-AMINOHEX-5-YNOIC ACID;L-HOMOPROPARGYLGLYCINE;H-HoMoGly(Propargyl)-OH;(S)-2-Amino-5-hexynoic acid;L-Homopropargylglycine (HPG)
• CAS NO: 98891-36-2
• Molecular Formula: C₆H₉NO₂
• Molecular Weight: 127.14
• Product Categories: Unusual Amino Acids
• Mol File: 98891-36-2.mol
• Article Data: 4

Chemical Properties

• Melting Point: 162°C
• Appearance: /
• Storage Temp.: -20°C
• Solubility: Aqueous Acid (Sparingly), Methanol (Slightly), Water (Slightly)
• Stability: Hygroscopic
• CAS DataBase Reference: (S)-2-AMINOHEX-5-YNOIC ACID(CAS DataBase Reference)
• NIST Chemistry Reference: (S)-2-AMINOHEX-5-YNOIC ACID(98891-36-2)
• EPA Substance Registry System: (S)-2-AMINOHEX-5-YNOIC ACID(98891-36-2)

Safety Data

• Hazardous Substances Data: 98891-36-2(Hazardous Substances Data)

Usage

Uses

Different sources of media describe the Uses of 98891-36-2 differently. You can refer to the following data:
1. L-Homopropargyl glycine is a reactive methionine analog that contains an alkyne moiety. It is readily inserted into newly-synthesized proteins in place of methionine. L-Homopropargyl glycine can then be labeled or captured through click chemistry. This approach represents a fast, sensitive, and non-radioactive alternative to [35S]-methionine for the detection of nascent protein synthesis.
2. L-Homopropargylglycine (HPG) is an amino acid analog of methionine that contains a very small modification, specifically an alkyne moiety. This compound can be fed to cultured cells and incorporated into proteins during active protein synthesis. Detection utilizes the chemoselective ligation or “click” reaction between an azide and an alkyne or cyclooctyne. For example the alkyne-modified protein can be detected with either fluorescent azide or biotin azide. Detection sensitivity with these reagents in 1-D gels and Western blots is in the low femtomole range and compatible with downstream LC-MS/MS and MALDI-MS analysis.

Upstream product

• 914367-68-3 N-acetyl-2-aminohex-5-ynoyc acid 
• 38771-21-0 4-bromobut-1-yne 
• 209474-96-4 diethyl α-acetamido-α-homopropargylmalonate 

Downstream Products

• 942518-21-0 2S-[[(9H-fluoren-9-ylmethoxy)carbonyl]amino]-5-hexynoic acid 
• 437553-87-2 (S)-N-[1-(tert-butyldimethylsilyloxymethyl)pent-4-ynyl]-4-methylbenzenesulfonamide 
• 437553-85-0 (S)-N-(1-hydroxymethylpent-4-ynyl)-4-methylbenzenesulfonamide 
• 540517-04-2 methyl (2S)-6-(2-aminophenyl)-2-[(tert-butoxycarbonyl)amino]-5-hexynoate 
• 437553-61-2 (S)-2-(toluene-4-sulfonylamino)hex-5-ynoic acid 
• 327-57-1 L-Norleucine 

Relevant articles and documents

Improved synthesis of unnatural amino acids for peptide stapling

The procedures for the synthesis of various α-alkenyl and alkyne amino acids were systematically optimized in light of enhancing atom economy, reducing hazardous reagent usage, and simplifying workup. By starting with Boc-Pro-OH and coupling with EDCI/DMAP followed by alkylation, chiral auxiliary was synthesized with high yield and enantioselectivity. For alkylation of the chiral complex, tBuONa was found and proved by quantitative calculation to be superior to tBuOK in generating more nucleophilic enolate salt, thereby can significantly enhance yield under room temperature. Final Fmoc protection was also dramatically facilitated in one-pot sequential manner by adding EDTA-2Na as the nickel chelator. Synthesis of α-bisalkenyl amino acid was also accomplished by achiral complex approach with high yield and efficacy. Accordingly, five most commonly used N-Fmoc protected α-alkenyl and alkynyl amino acids were synthesized and characterized.

A Biocatalytic Route to Enantiomerically Pure Unsaturated α-H-α-Amino Acids

A set of both enantiomeric forms of non-proteinogenic, unsaturated α-H-α-amino acids was efficiently synthesized using a biocatalytic pathway. This route involved the straightforward synthesis of the required unsaturated amino acid amides, followed by resolution with an aminopeptidase present in Pseudomonas putida ATCC 12633 and/or a genetically modified organism, leading to the (S)-acids and (R)-amides. Undesired amino acid racemase activity was identified in the wild-type strain, which was absent in the newly developed organism. The (R)-amides were hydrolyzed under mild conditions using an amidase present in whole cells from Rhodococcus erythropolis NCIMB 11540 to the (R)-acids. The viability of this procedure was demonstrated with the multi-gram synthesis of a variety of unsaturated amino acids in excellent enantiopurity.