Fmoc-3-(2'-quinoyl)-L-alanine
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Fmoc-3-(2'-quinoyl)-L-alanine

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Category
Fmoc-Amino Acids
Catalog number
BAT-007318
CAS number
214852-56-9
Molecular Formula
C27H22N2O4
Molecular Weight
438.48
Fmoc-3-(2'-quinoyl)-L-alanine
IUPAC Name
(2S)-2-(9H-fluoren-9-ylmethoxycarbonylamino)-3-quinolin-2-ylpropanoic acid
Synonyms
Fmoc-L-Ala(2'-quinolyl)-OH; Fmoc-(S)-2-Amino-3-quinolin-2-yl-propionic acid
Related CAS
214852-58-1 (D-isomer)
Appearance
White or off-white powder
Purity
≥ 99% (HPLC, TLC)
Density
1.325±0.06 g/cm3
Boiling Point
685.5±55.0 °C
Storage
Store at 2-8 °C
InChI
InChI=1S/C27H22N2O4/c30-26(31)25(15-18-14-13-17-7-1-6-12-24(17)28-18)29-27(32)33-16-23-21-10-4-2-8-19(21)20-9-3-5-11-22(20)23/h1-14,23,25H,15-16H2,(H,29,32)(H,30,31)/t25-/m0/s1
InChI Key
IDOMHXAHHXHYMO-VWLOTQADSA-N
Canonical SMILES
C1=CC=C2C(=C1)C=CC(=N2)CC(C(=O)O)NC(=O)OCC3C4=CC=CC=C4C5=CC=CC=C35

Fmoc-3-(2'-quinoyl)-L-alanine, a specialized amino acid derivative utilized in peptide synthesis and biochemical research, boasts diverse applications. Here are the key applications presented with high perplexity and burstiness:

Peptide Synthesis: Central to solid-phase peptide synthesis, Fmoc-3-(2'-quinoyl)-L-alanine plays a pivotal role in introducing quinoline-modified peptides. This strategic modification enhances peptide stability, biological activity, and binding properties. Scientists harness this derivative to craft peptides with tailored structural and functional attributes, catering to the demands of drug discovery and therapeutic endeavors.

Fluorescence Labeling: Owing to its quinoline moiety, Fmoc-3-(2'-quinoyl)-L-alanine serves as a versatile fluorescent probe in biological investigations. This capability enables real-time monitoring of peptide interactions and conformational dynamics. Fluorescently labeled peptides emerge as indispensable tools for unraveling molecular intricacies within cells and tissues, shedding light on fundamental biological processes.

Bioconjugation: Esteemed for its versatility, Fmoc-3-(2'-quinoyl)-L-alanine finds application in bioconjugation strategies, facilitating the coupling of peptides with diverse biomolecules like proteins, nucleic acids, and small compounds. This synergy enables the fabrication of multifunctional biomaterials pivotal in diagnostics, therapeutics, and nanotechnology. Bioconjugates bolster drug delivery precision, targeting efficacy, and therapeutic outcomes.

Structure-Activity Relationship Studies: By integrating Fmoc-3-(2'-quinoyl)-L-alanine into peptides, researchers embark on a journey of exploring structure-activity relationships. This deliberate manipulation of peptide sequences unveils key residues dictating biological activity, driving advancements in peptide design. These systematic studies form the bedrock for the rational development of peptide-based drugs and biomaterials, steering innovation in biopharmaceuticals and biomedical materials.

1. Engineering Corynebacterium glutamicum Mutants for 3-Methyl-1-butanol Production
Yu Zhang, Xiaohuan Zhang, Shiyuan Xiao, Wei Qi, Jingliang Xu, Zhenhong Yuan, Zhongming Wang Biochem Genet. 2019 Jun;57(3):443-454. doi: 10.1007/s10528-019-09906-4. Epub 2019 Jan 14.
3-Methyl-1-butanol (3MB) is a promising biofuel that can be produced from 2-ketoisocaproate via the common L-leucine biosynthesis pathway. Corynebacterium glutamicum was chosen as a host bacterium because of its strong resistance to isobutanol. In the current study, several strategies were designed to overproduce 3MB in C. glutamicum through a non-fermentation pathway. The engineered C. glutamicum mutant was obtained by silencing the pyruvate dehydrogenase gene complex (aceE) and deleting the lactic dehydrogenase gene (ldh), followed by mutagenesis with diethyl sulfate (DES) and selection with Fmoc-3-4-thiazolyl-L-alanine (FTA). The mutant could produce 659 mg/L of 3MB after 12 h of incubation. To facilitate carbon flux to 3MB biosynthesis, the engineered recombinant was also constructed without branched-chain acid aminotransferase (ilvE) activity by deleting the ilvE gene. This recombinant could produce 697 mg/L of 3MB after 12 h of incubation.
2. Biomimetic studies on the mechanism of stereoselective lanthionine formation
Yantao Zhu, Matt D Gieselman, Hao Zhou, Olga Averin, Wilfred A van der Donk Org Biomol Chem. 2003 Oct 7;1(19):3304-15. doi: 10.1039/b304945k.
Selenocysteine derivatives are useful precursors for the synthesis of peptide conjugates and selenopeptides. Several diastereomers of Fmoc-3-methyl-Se-phenylselenocysteine (FmocMeSec(Ph)) were prepared and used in solid phase peptide synthesis (SPPS). Once incorporated into peptides, the phenylselenide functionality provides a useful handle for the site and stereospecific introduction of E- or Z-dehydrobutyrine residues into peptide chains via oxidative elimination. The oxidation conditions are mild, can be performed on a solid support, and tolerate functionalities commonly found in peptides, including variously protected cysteine residues. Dehydropeptides containing unprotected cysteine residues undergo intramolecular stereoselective conjugate addition to afford cyclic lanthionines and methyllanthionines, which have the same stereochemistry as found in lantibiotics, a family of ribosomally synthesized and post-translationally modified peptide antibiotics. The observed stereoselectivity is shown to originate from a kinetic rather than a thermodynamic preference.
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