98891-36-2 Usage
Description
(S)-2-AMINOHEX-5-YNOIC ACID is a chiral compound that features an amino group and a terminal alkynyl group. It is a synthetic analog of the naturally occurring amino acid methionine, with the alkyne moiety providing unique reactivity and properties. (S)-2-AMINOHEX-5-YNOIC ACID is characterized by its ability to be readily incorporated into newly synthesized proteins in place of methionine, allowing for subsequent labeling or capture through click chemistry.
Uses
Used in Biochemistry Research:
(S)-2-AMINOHEX-5-YNOIC ACID is used as a reactive methionine analog for the detection of nascent protein synthesis. It is incorporated into proteins during active protein synthesis and can be labeled or captured through click chemistry, providing a fast, sensitive, and non-radioactive alternative to [35S]-methionine.
Used in Cell Culture Applications:
In cell culture, (S)-2-AMINOHEX-5-YNOIC ACID serves as an amino acid analog of methionine, which can be fed to cultured cells and incorporated into proteins. The detection of the alkyne-modified protein is achieved through chemoselective ligation or "click" reaction between an azide and an alkyne or cyclooctyne. This method allows for the use of fluorescent azide or biotin azide for detection, offering sensitivity in the low femtomole range and compatibility with downstream LC-MS/MS and MALDI-MS analysis.
Used in Drug Development:
(S)-2-AMINOHEX-5-YNOIC ACID can be utilized in the development of novel drug delivery systems and targeted therapies. Its unique reactivity and incorporation into proteins make it a valuable tool for the design of targeted drug conjugates and the study of protein-drug interactions.
Used in Chemical Biology:
(S)-2-AMINOHEX-5-YNOIC ACID is also used in chemical biology for the study of protein synthesis, post-translational modifications, and protein-protein interactions. Its alkyne functionality allows for the development of new bioorthogonal reactions and the exploration of novel chemical probes for biological systems.
Check Digit Verification of cas no
The CAS Registry Mumber 98891-36-2 includes 8 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 5 digits, 9,8,8,9 and 1 respectively; the second part has 2 digits, 3 and 6 respectively.
Calculate Digit Verification of CAS Registry Number 98891-36:
(7*9)+(6*8)+(5*8)+(4*9)+(3*1)+(2*3)+(1*6)=202
202 % 10 = 2
So 98891-36-2 is a valid CAS Registry Number.
98891-36-2Relevant articles and documents
Improved synthesis of unnatural amino acids for peptide stapling
Li, Bo,Zhang, Jie,Xu, Yongjuan,Yang, Xiaoxiao,Li, Li
supporting information, p. 2374 - 2377 (2017/05/29)
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
Wolf, Larissa B.,Sonke, Theo,Tjen, Kim C. M. F.,Kaptein, Bernard,Broxterman, Quirinus B.,Schoemaker, Hans E.,Rutjes, Floris P. J. T.
, p. 662 - 674 (2007/10/03)
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.
