Fmoc-His(3-Bom)-OH
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Fmoc-His(3-Bom)-OH

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Category
Fmoc-Amino Acids
Catalog number
BAT-003728
CAS number
84891-19-0
Molecular Formula
C29H27N3O5
Molecular Weight
497.56
Fmoc-His(3-Bom)-OH
IUPAC Name
(2S)-2-(9H-fluoren-9-ylmethoxycarbonylamino)-3-[3-(phenylmethoxymethyl)imidazol-4-yl]propanoic acid
Synonyms
Fmoc-L-His(p-Bom)-OH; Fmoc-N-p-benzyloxymethyl-L-histidine; (2S)-2-(9H-fluoren-9-ylmethoxycarbonylamino)-3-[3-(phenylmethoxymethyl)imidazol-4-yl]propanoic acid
Appearance
White powder
Purity
≥ 99% (HPLC)
Density
1.30±0.1 g/cm3
Boiling Point
757.7±60.0 °C
Storage
Store at 2-8 °C
InChI
InChI=1S/C29H27N3O5/c33-28(34)27(14-21-15-30-18-32(21)19-36-16-20-8-2-1-3-9-20)31-29(35)37-17-26-24-12-6-4-10-22(24)23-11-5-7-13-25(23)26/h1-13,15,18,26-27H,14,16-17,19H2,(H,31,35)(H,33,34)/t27-/m0/s1
InChI Key
CJBFCDKGOPEUOF-MHZLTWQESA-N
Canonical SMILES
C1=CC=C(C=C1)COCN2C=NC=C2CC(C(=O)O)NC(=O)OCC3C4=CC=CC=C4C5=CC=CC=C35
1. Synthesis and application of Nα-Fmoc-Nπ-4-methoxybenzyloxymethylhistidine in solid phase peptide synthesis
Hajime Hibino, Yasuyoshi Miki, Yuji Nishiuchi J Pept Sci. 2012 Dec;18(12):763-9. doi: 10.1002/psc.2464. Epub 2012 Oct 30.
The 4-methoxybenzyloxymethyl (MBom) group was introduced at the Nπ-position of the histidine (His) residue by using a regioselective procedure, and its utility was examined under standard conditions used for the conventional and the microwave (MW)-assisted solid phase peptide synthesis (SPPS) with 9-fluorenylmethyoxycarbonyl (Fmoc) chemistry. The Nπ-MBom group fulfilling the requirements for the Fmoc strategy was found to prevent side-chain-induced racemization during incorporation of the His residue even in the case of MW-assisted SPPS performed at a high temperature. In particular, the MBom group proved to be a suitable protecting group for the convergent synthesis because it remains attached to the imidazole ring during detachment of the protected His-containing peptide segments from acid-sensitive linkers by treatment with a weak acid such as 1% trifluoroacetic acid in dichloromethane. We also demonstrated the facile synthesis of Fmoc-His(π-MBom)-OH with the aid of purification procedure by crystallization to effectively remove the undesired τ-isomer without resorting to silica gel column chromatography. This means that the present synthetic procedure can be used for large-scale production without any obstacles.
2. A 'conovenomic' analysis of the milked venom from the mollusk-hunting cone snail Conus textile--the pharmacological importance of post-translational modifications
Zachary L Bergeron, et al. Peptides. 2013 Nov;49:145-58. doi: 10.1016/j.peptides.2013.09.004. Epub 2013 Sep 18.
Cone snail venoms provide a largely untapped source of novel peptide drug leads. To enhance the discovery phase, a detailed comparative proteomic analysis was undertaken on milked venom from the mollusk-hunting cone snail, Conus textile, from three different geographic locations (Hawai'i, American Samoa and Australia's Great Barrier Reef). A novel milked venom conopeptide rich in post-translational modifications was discovered, characterized and named α-conotoxin TxIC. We assign this conopeptide to the 4/7 α-conotoxin family based on the peptide's sequence homology and cDNA pre-propeptide alignment. Pharmacologically, α-conotoxin TxIC demonstrates minimal activity on human acetylcholine receptor models (100 μM, <5% inhibition), compared to its high paralytic potency in invertebrates, PD50 = 34.2 nMol kg(-1). The non-post-translationally modified form, [Pro](2,8)[Glu](16)α-conotoxin TxIC, demonstrates differential selectivity for the α3β2 isoform of the nicotinic acetylcholine receptor with maximal inhibition of 96% and an observed IC50 of 5.4 ± 0.5 μM. Interestingly its comparative PD50 (3.6 μMol kg(-1)) in invertebrates was ~100 fold more than that of the native peptide. Differentiating α-conotoxin TxIC from other α-conotoxins is the high degree of post-translational modification (44% of residues). This includes the incorporation of γ-carboxyglutamic acid, two moieties of 4-trans hydroxyproline, two disulfide bond linkages, and C-terminal amidation. These findings expand upon the known chemical diversity of α-conotoxins and illustrate a potential driver of toxin phyla-selectivity within Conus.
3. Synthesis and application of Fmoc-His(3-Bum)-OH
M Mergler, F Dick, B Sax, J Schwindling, T H Vorherr J Pept Sci. 2001 Sep;7(9):502-10. doi: 10.1002/psc.345.
This paper presents a reevaluation of the synthesis and properties of Fmoc-His(3-Bum)-OH regarding its application in SPPS with minimal racemization of histidine residues during coupling and esterification reactions. By-product formation during the deprotection of the test peptides could be significantly reduced by scavenging the concomitantly formed HCHO, e.g. with methoxyamine.
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