Boc-Thr(Leu-Fmoc)-OH
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Boc-Thr(Leu-Fmoc)-OH

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Category
Functional Peptides
Catalog number
BAT-001409
CAS number
944283-26-5
Molecular Formula
C30H38N2O8
Molecular Weight
554.64
IUPAC Name
(2S,3R)-3-[(2S)-2-(9H-fluoren-9-ylmethoxycarbonylamino)-4-methylpentanoyl]oxy-2-[(2-methylpropan-2-yl)oxycarbonylamino]butanoic acid
Synonyms
Boc-L-Thr(Leu-Fmoc)-OH; (2S,3R)-3-[(2S)-2-(9H-fluoren-9-ylmethoxycarbonylamino)-4-methylpentanoyl]oxy-2-[(2-methylpropan-2-yl)oxycarbonylamino]butanoic acid
Appearance
White to off-white powder
Purity
≥ 98% (HPLC)
Density
1.2±0.1 g/cm3
Boiling Point
735.8±60.0 °C at 760 mmHg
Storage
Store at -20 °C
InChI
InChI=1S/C30H38N2O8/c1-17(2)15-24(27(35)39-18(3)25(26(33)34)32-29(37)40-30(4,5)6)31-28(36)38-16-23-21-13-9-7-11-19(21)20-12-8-10-14-22(20)23/h7-14,17-18,23-25H,15-16H2,1-6H3,(H,31,36)(H,32,37)(H,33,34)/t18-,24+,25+/m1/s1
InChI Key
RRBJZTPVMBBJNT-YWWLGCSWSA-N
Canonical SMILES
CC(C)CC(C(=O)OC(C)C(C(=O)O)NC(=O)OC(C)(C)C)NC(=O)OCC1C2=CC=CC=C2C3=CC=CC=C13
1. Synthesis and biological activity of some linear and cyclic kinin analogues
M Gobbo, L Biondi, F Filira, R Rocchi, T Piek Int J Pept Protein Res. 1994 Jul;44(1):1-9. doi: 10.1111/j.1399-3011.1994.tb00397.x.
Syntheses are described of some linear and cyclic kinin analogues. Cyclization, by the diphenyl-phosphorazide method, of linear peptides prepared by the solid-phase procedure based on Fmoc chemistry, was used for preparing cyclo-bradykinin and cyclo-kallidin (cyclo-Lys-bradykinin). Removal of the protecting group from the lysine side chain of cyclo-kallidin followed by acylation with the N-terminal sequence of vespulakinin 1 (VSK 1), Fmoc-Thr(tBu)-Ala-Thr(tBu)-Thr(tBu)-Arg(Pmc)-Arg(Pmc)-Gly-OH, by the Bop-HOBt procedure, yielded the protected N epsilon-(1-8 VSK 1)-cyclo-N alpha-kallidin, which was deblocked by acid treatment and purified by semi-preparative HPLC. The diglycosylated 1-8 VSK 1 sequence Boc-Thr(tBu)-Ala-(Gal beta)Thr-(Gal beta)Thr-Arg(Pmc)-Arg(Pmc)-Gly-OH was also synthesized by the solid-phase procedure and used to prepare the N epsilon-[(Gal beta)Thr3, (Gal beta)Thr4, 1-8 VSK 1]-cyclo-N-alpha- kallidin. Peptides and glycopeptides were characterized by amino acid analysis, optical rotation, analytical HPLC and FAB-MS. Preliminary pharmacological experiments showed that the cyclic kinin analogues are much less potent then bradykinin but still show specific bradykinin-like actions that support the hypothesis of the presence of a pharmacophore in the centre of the (brady)kinin molecule.
2. Synthesis of modified tuftsins containing monosaccharides or monosaccharide derivatives
R Rocchi, L Biondi, F Filira, M Gobbo, S Dagan, M Fridkin Int J Pept Protein Res. 1987 Feb;29(2):250-61. doi: 10.1111/j.1399-3011.1987.tb02252.x.
Synthesis of some modified tuftsins is described in which a monosaccharide or a monosaccharide derivative was incorporated in the molecule. Acylation of H-Thr-Lys(Z)-Pro-Arg(NO2)-OBzl with D(+)-gluco-1,5-lactone followed by catalytic hydrogenation gave N alpha-gluconyl-tuftsin. Glycosylation of the carboxyl function of the C-terminal arginine has been achieved by reacting, through the mixed anhydride procedure, Boc-Thr-Lys(Z)-Pro-OH with 2-deoxy-2-(NG-nitroargininamido)-D-glucopyranose followed by catalytic hydrogenation and trifluoroacetic acid treatment. O-Glucosyl-tuftsin has been prepared by reacting o-nitrophenyl N-benzyloxycarbonyl-O-[(alpha + beta) 2,3,4,6-tetra-O-benzyl-D-glucopyranosyl]-threoninate with H-Lys(Z)-Pro-Arg(NO2)-OBzl in the presence of 1-hydroxybenzotriazole. Flash chromatography on silica gel allowed a partial separation of the diastereoisomers, one of which has been isolated in a reasonable yield. The single diastereoisomer and the alpha + beta anomeric mixture were separately deblocked by catalytic hydrogenation and purified by RP-HPLC.
3. Efficient solution phase synthesis and use of multiple O-phosphothreonyl-containing peptides for calcium phosphate binding studies
J W Perich, D P Kelly, E C Reynolds Int J Pept Protein Res. 1993 Mar;41(3):275-81. doi: 10.1111/j.1399-3011.1993.tb00335.x.
The protected phosphothreonine derivative Boc-Thr(PO3Ph2)-OH was prepared in high yield from Boc-Thr-OH by a simple three-step procedure which involved 4-nitrobenzylcarboxyl protection, either phosphorotriester (diphenyl phosphorochloridate) or "phosphite-triester" (diphenyl N,N-diethylphosphoramidite) phosphorylation of the threonine hydroxyl group of Boc-Thr-ONb followed by hydrogenolytic carboxyl deprotection. The three Thr(P)-containing peptides, H-Thr(P)-Glu-Glu-NHMe.TFA, H-Thr(P)-Thr(P)-Glu-Glu-NHMe.TFA and H-Thr(P)-Thr(P)-Thr(P)-Glu-Glu-NHMe.TFA, were prepared in high yield by the use of Boc-Thr(PO3Ph2)-OH in the Boc mode of peptide synthesis (mixed anhydride method) followed by platinum-mediated hydrogenolytic deprotection of the Thr(PO3Ph2)-containing peptides. The use of the phosphopeptides in calcium phosphate binding studies showed that the triple Thr(P)-cluster was a basic structural requirement, since only the pentapeptide was able to bind calcium phosphate efficiently.
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