Fmoc-Phe-Ser[Psi(Me,Me)Pro]-OH
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Fmoc-Phe-Ser[Psi(Me,Me)Pro]-OH

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Category
Others
Catalog number
BAT-007682
CAS number
878797-01-4
Molecular Formula
C30H30N2O6
Molecular Weight
514.58
Fmoc-Phe-Ser[Psi(Me,Me)Pro]-OH
IUPAC Name
(4S)-3-[(2S)-2-(9H-fluoren-9-ylmethoxycarbonylamino)-3-phenylpropanoyl]-2,2-dimethyl-1,3-oxazolidine-4-carboxylic acid
Synonyms
Fmoc-Phe-Ser[Ψ(Me,Me)Pro]-OH; (S)-3-[N-(9-Fluorenylmethyloxycarbonyl)-L-phenylalaninyl]-2,2-dimethyloxazolidine-4-carboxylic acid; Fmoc-Phe-Ser(Psime,Mepro)-OH; Fmoc-L-Phe-L-Ser(Psi(Me,Me)pro)-OH; AS-59642; (4S)-3-[(2S)-2-({[(9H-fluoren-9-yl)methoxy]carbonyl}amino)-3-phenylpropanoyl]-2,2-dimethyl-1,3-oxazolidine-4-carboxylic acid
Appearance
White to off-white powder
Purity
≥ 99% (HPLC, TLC)
Density
1.286±0.06 g/cm3 (Predicted)
Boiling Point
765.5±60.0 °C (Predicted)
Storage
Store at -20 °C
InChI
InChI=1S/C30H30N2O6/c1-30(2)32(26(18-38-30)28(34)35)27(33)25(16-19-10-4-3-5-11-19)31-29(36)37-17-24-22-14-8-6-12-20(22)21-13-7-9-15-23(21)24/h3-15,24-26H,16-18H2,1-2H3,(H,31,36)(H,34,35)/t25-,26-/m0/s1
InChI Key
PQJUKTSKOYOXMZ-UIOOFZCWSA-N
Canonical SMILES
CC1(N(C(CO1)C(=O)O)C(=O)C(CC2=CC=CC=C2)NC(=O)OCC3C4=CC=CC=C4C5=CC=CC=C35)C
1. Epimerization-Free Preparation of C-Terminal Cys Peptide Acid by Fmoc SPPS Using Pseudoproline-Type Protecting Group
Shugo Tsuda, Shun Masuda, Taku Yoshiya J Org Chem. 2020 Feb 7;85(3):1674-1679. doi: 10.1021/acs.joc.9b02344. Epub 2019 Oct 31.
Preparation of C-terminal Cys-containing peptide acid by Fmoc solid-phase peptide synthesis (SPPS) is difficult due to base-mediated epimerization at Cys. In this paper, use of a C-terminal pseudoproline structure and Trt(2-Cl) resin achieved epimerization-free direct preparation of the C-terminal Cys-containing peptide acid by Fmoc SPPS. Additionally, the C-terminal Cys(ΨDmp,Hpro)-containing protected peptide segment was applied to an epimerization-free segment condensation reaction.
2. Chemoselective Disulfide Formation by Thiol-Disulfide Interchange in SIT-Protected Cysteinyl Peptides
Amit Chakraborty, Fernando Albericio, Beatriz G de la Torre J Org Chem. 2022 Jan 7;87(1):708-712. doi: 10.1021/acs.joc.1c02705. Epub 2021 Dec 15.
Chemoselective disulfide formation is accomplished through a thiol-disulfide interchange approach using sec-isoamyl mercaptan (SIT) as an alkyl sulfenyl-protecting group of one of the Cys residues involved in the pairing. SIT has a dual and unique characteristic, acting as a masking group during the synthesis and directing disulfide formation in the presence of a free thiol. This novel approach is illustrated by the synthesis of several peptides of biological interest.
3. An unnatural amino acid that induces beta-sheet folding and interaction in peptides
James S Nowick, Kit S Lam, Tatyana V Khasanova, William E Kemnitzer, Santanu Maitra, Hao T Mee, Ruiwu Liu J Am Chem Soc. 2002 May 8;124(18):4972-3. doi: 10.1021/ja025699i.
This paper introduces a unique amino acid that can readily be incorporated into peptides to make them fold into beta-sheetlike structures that dimerize through beta-sheet interactions. This new amino acid, Orn(i-PrCO-Hao), consists of an ornithine residue with the beta-strand-mimicking amino acid Hao [J. Am. Chem. Soc. 2000, 122, 7654-7661] attached to its side chain. When Orn(i-PrCO-Hao) is incorporated into a peptide, or appended to its N-terminus, the Hao group hydrogen bonds to the three subsequent residues to form a beta-sheetlike structure. The amino acid Orn(i-PrCO-Hao) is readily used in peptide synthesis as its Fmoc derivative, Fmoc-Orn(i-PrCO-Hao)-OH (3). Fmoc-Orn(i-PrCO-Hao)-OH behaves like a regular amino acid in peptide synthesis and was uneventfully incorporated into the peptide o-anisoyl-Val-Orn(i-PrCO-Hao)-Phe-Ile-Leu-NHMe (4) through standard automated Fmoc solid-phase peptide synthesis, with DIC and HOAt as the coupling agent for Fmoc-Orn(i-PrCO-Hao)-OH and o-anisic acid and HATU as the coupling agent for all other couplings. A second synthetic strategy was developed to facilitate the preparation of peptides with N-terminal Orn(i-PrCO-Hao) residues, which avoids the need for the preparation of Fmoc-Orn(i-PrCO-Hao)-OH. In this strategy, Boc-Orn(Fmoc)-OH is used as the penultimate amino acid in the peptide synthesis, and i-PrCO-Hao-OH (2) is used as the final amino acid. N-Terminal Orn(i-PrCO-Hao) peptide H-Orn(i-PrCO-Hao)-Phe-Ile-Leu-NHMe.TFA (5) was prepared in a fashion similar to that for 4, using DIC and HOAt as the coupling agent for i-PrCO-Hao-OH and HATU as the coupling agent for all other couplings. 1H NMR transverse-ROESY, coupling constant, and chemical shift studies establish that peptide 4 forms a dimeric beta-sheetlike structure in CDCl3 solution. The 1H NMR studies also suggest that the ornithine unit adopts a well-defined turn conformation. Analogous 1H NMR studies of peptide 5 indicate that this TFA salt folds but does not dimerize in CD3OD solution. Collectively, these synthetic and spectroscopic studies establish that the amino acid Orn(i-PrCO-Hao) induces beta-sheet structure and interactions in peptides in suitable organic solvents. Unlike the Hao amino acid, which acts as a prosthetic to replace three residues of the peptide strand, the Orn(i-PrCO-Hao) amino acid acts as a splint that helps enforce a beta-sheetlike structure without replacing the residues and their side chains. This feature of Orn(i-PrCO-Hao) is important, because it allows the creation of beta-sheet structure with minimal perturbation of the peptide sequence.
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