L-Histidine amide dihydrochloride
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L-Histidine amide dihydrochloride

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Category
L-Amino Acids
Catalog number
BAT-003977
CAS number
71666-95-0
Molecular Formula
C6H10N4O·2HCl
Molecular Weight
227.20
L-Histidine amide dihydrochloride
IUPAC Name
(2S)-2-amino-3-(1H-imidazol-5-yl)propanamide;dihydrochloride
Synonyms
H-His-NH2 2HCl; 1H-Imidazole-4-propanamide,a-amino-,dihydrochloride,(S)
Appearance
White powder
Purity
≥ 99% (TLC)
Storage
Store at 2-8 °C
InChI
InChI=1S/C6H10N4O.2ClH/c7-5(6(8)11)1-4-2-9-3-10-4;;/h2-3,5H,1,7H2,(H2,8,11)(H,9,10);2*1H/t5-;;/m0../s1
InChI Key
CRBYFJCXMZNLTO-XRIGFGBMSA-N
Canonical SMILES
C1=C(NC=N1)CC(C(=O)N)N.Cl.Cl
1. Small interfering RNA for cancer treatment: overcoming hurdles in delivery
Nitin Bharat Charbe, et al. Acta Pharm Sin B. 2020 Nov;10(11):2075-2109. doi: 10.1016/j.apsb.2020.10.005. Epub 2020 Oct 13.
In many ways, cancer cells are different from healthy cells. A lot of tactical nano-based drug delivery systems are based on the difference between cancer and healthy cells. Currently, nanotechnology-based delivery systems are the most promising tool to deliver DNA-based products to cancer cells. This review aims to highlight the latest development in the lipids and polymeric nanocarrier for siRNA delivery to the cancer cells. It also provides the necessary information about siRNA development and its mechanism of action. Overall, this review gives us a clear picture of lipid and polymer-based drug delivery systems, which in the future could form the base to translate the basic siRNA biology into siRNA-based cancer therapies.
3. Energetics-based methods for protein folding and stability measurements
M Ariel Geer, Michael C Fitzgerald Annu Rev Anal Chem (Palo Alto Calif). 2014;7:209-28. doi: 10.1146/annurev-anchem-071213-020024. Epub 2014 May 28.
Over the past 15 years, a series of energetics-based techniques have been developed for the thermodynamic analysis of protein folding and stability. These techniques include Stability of Unpurified Proteins from Rates of amide H/D Exchange (SUPREX), pulse proteolysis, Stability of Proteins from Rates of Oxidation (SPROX), slow histidine H/D exchange, lysine amidination, and quantitative cysteine reactivity (QCR). The above techniques, which are the subject of this review, all utilize chemical or enzymatic modification reactions to probe the chemical denaturant- or temperature-induced equilibrium unfolding properties of proteins and protein-ligand complexes. They employ various mass spectrometry-, sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE)-, and optical spectroscopy-based readouts that are particularly advantageous for high-throughput and in some cases multiplexed analyses. This has created the opportunity to use protein folding and stability measurements in new applications such as in high-throughput screening projects to identify novel protein ligands and in mode-of-action studies to identify protein targets of a particular ligand.
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