Boc-L-aspartic acid α-cyclohexyl ester dicyclohexylammonium salt
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Boc-L-aspartic acid α-cyclohexyl ester dicyclohexylammonium salt

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Category
BOC-Amino Acids
Catalog number
BAT-004529
CAS number
200283-00-7
Molecular Formula
C15H25NO6·C12H23N
Molecular Weight
496.70
Boc-L-aspartic acid α-cyclohexyl ester dicyclohexylammonium salt
IUPAC Name
N-cyclohexylcyclohexanamine;(3S)-4-cyclohexyloxy-3-[(2-methylpropan-2-yl)oxycarbonylamino]-4-oxobutanoic acid
Synonyms
Boc-L-Asp-OcHex DCHA
Appearance
White powder
Purity
≥ 98% (TLC)
Melting Point
151-160 °C
Storage
Store at 2-8 °C
InChI
InChI=1S/C15H25NO6.C12H23N/c1-15(2,3)22-14(20)16-11(9-12(17)18)13(19)21-10-7-5-4-6-8-10;1-3-7-11(8-4-1)13-12-9-5-2-6-10-12/h10-11H,4-9H2,1-3H3,(H,16,20)(H,17,18);11-13H,1-10H2/t11-;/m0./s1
InChI Key
GUAPOQKXUJIYAF-MERQFXBCSA-N
Canonical SMILES
CC(C)(C)OC(=O)NC(CC(=O)O)C(=O)OC1CCCCC1.C1CCC(CC1)NC2CCCCC2

Boc-L-aspartic acid α-cyclohexyl ester dicyclohexylammonium salt, a specialized chemical compound with diverse bioscience applications, is utilized in various cutting-edge fields. Here are four key applications presented with high perplexity and burstiness:

Peptide Synthesis: Playing a pivotal role in peptide synthesis, this compound serves as a protected amino acid derivative essential for seamless peptide bond formation. Its Boc protective group shields against unwanted reactions at the amino group, ensuring precise sequential synthesis. The salt form augments solubility and stability, simplifying handling during the synthesis journey.

Drug Development: In the realm of pharmaceutical investigations, Boc-L-aspartic acid α-cyclohexyl ester dicyclohexylammonium salt shines as a catalyst for crafting bespoke peptide sequences with therapeutic potential. Researchers harness its properties to synthesize peptides capable of modulating vital biological targets, expediting the development of novel medicines. Its precise integration into peptide chains unlocks insights into structure-activity relationships, crucial for innovative drug design.

Protein Engineering: A linchpin in protein engineering endeavors, this compound empowers the integration of non-natural amino acids into protein sequences. This breakthrough enables the introduction of specific functional groups, facilitating in-depth studies on protein behavior, stability, and interactions. This application is instrumental in unraveling protein mechanisms and designing advanced proteins tailored for diverse applications.

Bioconjugation: At the forefront of bioconjugation methodologies, Boc-L-aspartic acid α-cyclohexyl ester dicyclohexylammonium salt plays a pivotal role in linking peptides or small molecules to larger biomolecules like antibodies or enzymes. Its safeguarded form ensures selective modification at targeted sites without disrupting other functional groups. This precision is paramount in crafting targeted delivery systems, diagnostic tools, and therapeutic agents.

1.GABAergic Pharmacotherapy in the Treatment of Motor Disorders of the Central Nervous System.
Gazulla J1, Ruiz-Gazulla C, Tintore M. Curr Pharm Des. 2015;21(34):4989-95.
Gamma-aminobutyric acid (GABA) is the main inhibitory neurotransmitter in the central nervous system, and diseases that associate a deficiency in GABA might benefit from GABAergic drugs. Cerebellar Purkinje cells employ GABA as a neurotransmitter. Cortical cerebellar atrophy (CCA) shows Purkinje cell loss, and ataxia caused by it was alleviated by gabapentin and pregabalin. Thus, CCA is proposed as a model of selective deficiency in GABA in the cerebellum, which benefits clinically from administration of GABAergic drugs, in a manner similar in which levodopa improves motor manifestations in Parkinson's disease. Other ataxias also benefited clinically from GABAergic drugs, as adult-onset GM2 gangliosidosis, olivopontocerebellar atrophy, cerebellar ataxia with hypogonadism, spinocerebellar ataxias 1, 2 and 6, and adult-onset ataxia-telangiectasia. Complex neurochemical diseases, as multiple-system atrophy, had ataxia worsened by GABAergic drugs.
2.Insights into the mechanism of C5aR inhibition by PMX53 via implicit solvent molecular dynamics simulations and docking.
Tamamis P1, Kieslich CA2, Nikiforovich GV3, Woodruff TM4, Morikis D2, Archontis G1. BMC Biophys. 2014 Aug 12;7:5. doi: 10.1186/2046-1682-7-5. eCollection 2014.
BACKGROUND: The complement protein C5a acts by primarily binding and activating the G-protein coupled C5a receptor C5aR (CD88), and is implicated in many inflammatory diseases. The cyclic hexapeptide PMX53 (sequence Ace-Phe-[Orn-Pro-dCha-Trp-Arg]) is a full C5aR antagonist of nanomolar potency, and is widely used to study C5aR function in disease.
3.No Habitat Selection during Spring Migration at a Meso-Scale Range across Mosaic Landscapes: A Case Study with the Woodcock (Scolopax rusticola).
Crespo A1, Rodrigues M2, Telletxea I3, Ibáñez R3, Díez F3, Tobar JF3, Arizaga J1. PLoS One. 2016 Mar 22;11(3):e0149790. doi: 10.1371/journal.pone.0149790. eCollection 2016.
Success of migration in birds in part depends on habitat selection. Overall, it is still poorly known whether there is habitat selection amongst landbird migrants moving across landscapes. Europe is chiefly covered by agro-forestry mosaic landscapes, so migratory species associated to either agricultural landscapes or woodland habitats should theoretically find suitable stopover sites along migration. During migration from wintering to breeding quarters, woodcocks (Scolopax rusticola) tagged with PTT satellite-tracking transmitters were used to test for the hypothesis that migrants associated to agro-forest habitats have no habitat selection during migration, at a meso-scale level. Using a GIS platform we extracted at a meso-scale range habitat cover at stopover localities. Results obtained from comparisons of soil covers between points randomly selected and true stopover localities sites revealed, as expected, the species may not select for particular habitats at a meso-scale range, because the habitat (or habitats) required by the species can be found virtually everywhere on their migration route.
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