Boc-D-β-iodo-Ala-OMe
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Boc-D-β-iodo-Ala-OMe

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Category
BOC-Amino Acids
Catalog number
BAT-000823
CAS number
93267-04-0
Molecular Formula
C9H16INO4
Molecular Weight
329.1
Boc-D-β-iodo-Ala-OMe
IUPAC Name
methyl (2R)-3-iodo-2-[(2-methylpropan-2-yl)oxycarbonylamino]propanoate
Synonyms
Boc-beta-iodo-Ala-OMe; Boc-3-iodo-L-alanine methyl ester; (R)-Methyl 2-((tert-butoxycarbonyl)amino)-3-iodopropanoate; N-(tert-Butoxycarbonyl)-3-iodo-L-alanine methyl ester
Appearance
White fine crystals
Purity
95%
Density
1.551 g/cm3
Melting Point
50-52 °C (lit.)
Boiling Point
356.5°C at 760 mmHg
Storage
Store at 2-8 °C
InChI
InChI=1S/C9H16INO4/c1-9(2,3)15-8(13)11-6(5-10)7(12)14-4/h6H,5H2,1-4H3,(H,11,13)/t6-/m0/s1
InChI Key
UGZBFCCHLUWCQI-LURJTMIESA-N
Canonical SMILES
CC(C)(C)OC(=O)NC(CI)C(=O)OC

Boc-D-β-iodo-Ala-OMe, a synthetic peptide derivative, finds diverse applications in biochemical and pharmaceutical research. Here are the key applications intricately presented with high perplexity and burstiness:

Peptide Synthesis: Serving as a foundational element in peptide synthesis, Boc-D-β-iodo-Ala-OMe integrates into peptide chains, enabling the introduction of iodinated residues. These residues prove invaluable for subsequent chemical alterations or for monitoring peptide interactions through radiolabeling techniques. This capability empowers the creation of tailor-made peptides with precise functional attributes, tailored for intricate research endeavors.

Chemical Biology: Within the realm of chemical biology, Boc-D-β-iodo-Ala-OMe emerges as a versatile tool for probing protein structure and function. The iodine atom acts as a focal point for cross-linking or binding interactions with other chemical groups, facilitating the exploration of protein interactions and conformations. This methodology is pivotal for unraveling protein mechanisms and devising inhibitors or activators for therapeutic targets with nuanced effectiveness.

Radiopharmaceuticals: Exploiting its potential in radiopharmaceutical development, Boc-D-β-iodo-Ala-OMe contributes to imaging and diagnostic applications. By substituting the iodine moiety with radioactive isotopes, researchers can track the distribution and localization of peptides within biological systems. This capability proves particularly valuable in diagnosing and monitoring diseases such as cancer with exceptional precision.

Drug Development: As a pivotal player in drug development, this peptide derivative serves as both a lead compound and a scaffold for formulating novel therapeutics. The distinctive structural attributes of Boc-D-β-iodo-Ala-OMe open avenues for exploring uncharted chemical spaces and refining drug-like properties. Researchers wield the power to modify this compound, optimizing its activity, selectivity, and pharmacokinetic profiles for enhanced therapeutic efficacy.

1.(7-Diethylaminocoumarin-4-yl)methyl ester of suberoylanilide hydroxamic acid as a caged inhibitor for photocontrol of histone deacetylase activity.
Ieda N1, Yamada S2, Kawaguchi M1, Miyata N1, Nakagawa H3. Bioorg Med Chem. 2016 Apr 22. pii: S0968-0896(16)30285-1. doi: 10.1016/j.bmc.2016.04.042. [Epub ahead of print]
Histone deacetylases (HDACs) are involved in epigenetic control of the expression of various genes by catalyzing deacetylation of ε-acetylated lysine residues. Here, we report the design, synthesis and evaluation of the (7-diethylaminocoumarin-4-yl)methyl ester of suberoylanilide hydroxamic acid (AC-SAHA) as a caged HDAC inhibitor, which releases the known pan-HDAC inhibitor SAHA upon cleavage of the photolabile (7-diethylaminocoumarin-4-yl)methyl protecting group in response to photoirradiation. A key advantage of AC-SAHA is that the caged derivative itself shows essentially no HDAC-inhibitory activity. Upon photoirradiation, AC-SAHA decomposes to SAHA and a 7-diethylaminocoumarin derivative, together with some minor products. We confirmed that AC-SAHA inhibits HDAC in response to photoirradiation in vitro by means of chemiluminescence assay. AC-SAHA also showed photoinduced inhibition of proliferation of human colon cancer cell line HCT116, as determined by MTT assay.
2.Chikusetsusaponin IVa Methyl Ester Isolated from the Roots of Achyranthes japonica Suppresses LPS-Induced iNOS, TNF-α, IL-6, and IL-1β Expression by NF-κB and AP-1 Inactivation.
Lee HJ1, Shin JS, Lee WS, Shim HY, Park JM, Jang DS, Lee KT. Biol Pharm Bull. 2016;39(5):657-64. doi: 10.1248/bpb.b15-00572.
We investigated the effect of chikusetsusaponin IVa (CS) and chikusetsusaponin IVa methyl ester (CS-ME) from the roots of Achyranthes japonica NAKAI on lipopolysaccharide (LPS)-induced nitric oxide (NO) and prostaglandin E2 (PGE2) production in RAW264.7 macrophages. CS-ME more potently inhibited LPS-induced NO and PGE2 production than CS. CS-ME concentration-dependently inhibited LPS-induced tumor necrosis factor (TNF)-α and interleukin (IL)-6 and IL-1β production in RAW264.7 macrophages and mouse peritoneal macrophages. Consistent with these findings, CS-ME suppressed LPS-induced expression of inducible NO synthase (iNOS) and cyclooxygenase (COX)-2 at protein level as well as iNOS, COX-2, TNF-α, IL-6, and IL-1β at mRNA level. In addition, CS-ME suppressed LPS-induced transcriptional activity of nuclear factor (NF)-κB and activator protein (AP)-1. The anti-inflammatory properties of CS-ME might result from suppression of iNOS, COX-2, TNF-α, IL-6, and IL-1β expression through downregulation of NF-κB and AP-1 in macrophages.
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