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Application Area

Fmoc-N-Me-D-Asp(Ompe)-OH

* Please kindly note that our products are not to be used for therapeutic purposes and cannot be sold to patients.

Category

Fmoc-Amino Acids

Catalog number

BAT-009005

Molecular Formula

C26H31NO6

Molecular Weight

453.53

Synonyms

(R)-2-((((9H-fluoren-9-yl)methoxy)carbonyl)(methyl)amino)-4-((3-methylpentan-3-yl)oxy)-4-oxobutanoic acid

Fmoc-N-Me-D-Asp(Ompe)-OH is a specialized amino acid derivative used in peptide synthesis and biochemical research. Here are some key applications of Fmoc-N-Me-D-Asp(Ompe)-OH:

Peptide Synthesis: Fmoc-N-Me-D-Asp(Ompe)-OH is commonly used in the solid-phase synthesis of peptides. The Fmoc protecting group allows for easy addition of this amino acid derivative into growing peptide chains while preventing undesirable side reactions. This makes it particularly useful for synthesizing complex peptides with precise sequences and modifications.

Structural Biology: In structural biology, Fmoc-N-Me-D-Asp(Ompe)-OH is used to introduce specific conformations in peptides and proteins. The presence of the N-Me group can induce unique folding patterns, which helps in studying protein structure and function. These modifications are valuable in determining the relationship between protein structure and its biological activity.

Drug Design: Researchers use Fmoc-N-Me-D-Asp(Ompe)-OH in drug design to develop peptide-based therapeutics. By incorporating this amino acid derivative into peptide sequences, scientists can enhance the binding affinity, stability, and specificity of potential drug candidates. This approach is crucial in creating effective and targeted treatments for various diseases.

Biophysical Studies: Fmoc-N-Me-D-Asp(Ompe)-OH is employed in biophysical studies to investigate peptide interactions with membranes, proteins, or other biomolecules. The structural features of this amino acid derivative can mimic natural interactions, helping researchers understand the dynamics and mechanisms of biological processes. These insights are essential for developing new biotechnological applications and therapeutic strategies.

1. New t-butyl based aspartate protecting groups preventing aspartimide formation in Fmoc SPPS

Raymond Behrendt, Simon Huber, Roger Martí, Peter White J Pept Sci. 2015 Aug;21(8):680-7. doi: 10.1002/psc.2790. Epub 2015 Jun 15.

Obtaining homogenous aspartyl-containing peptides via Fmoc/tBu chemistry is often an insurmountable obstacle. A generic solution for this issue utilising an optimised side-chain protection strategy that minimises aspartimide formation would therefore be most desirable. To this end, we developed the following new derivatives: Fmoc-Asp(OEpe)-OH (Epe = 3-ethyl-3-pentyl), Fmoc-Asp(OPhp)-OH (Php = 4-n-propyl-4-heptyl) and Fmoc-Asp(OBno)-OH (Bno = 5-n-butyl-5-nonyl). We have compared their effectiveness against that of Fmoc-Asp(OtBu)-OH and Fmoc-Asp(OMpe)-OH in the well-established scorpion toxin II model peptide variants H-Val-Lys-Asp-Asn/Arg-Tyr-Ile-OH by treatments of the peptidyl resins with the Fmoc removal reagents containing piperidine and DBU at both room and elevated temperatures. The new derivatives proved to be extremely effective in minimising aspartimide by-products in each application.

2. The aspartimide problem in Fmoc-based SPPS. Part III

M Mergler, F Dick J Pept Sci. 2005 Oct;11(10):650-7. doi: 10.1002/psc.668.

A newly developed Fmoc-Asp derivative, Fmoc-Asp beta-(2,3,4-trimethyl-pent-3-yl) ester, has been tried in the Fmoc-based SPPS of H-Val-Lys-Asp-Xaa-Tyr-Ile-OH, a well-established peptide model for studying base-catalysed aspartimide formation. When synthesizing the hexapeptide incorporating Gly, Arg(Pbf), Asn(Mtt), Asp(OtBu) or Cys(Acm) for Xaa, considerable amounts of aspartimide-related by-products were to be expected. The Asp(3) beta-carboxy protecting group and the duration of exposure to bases were varied. By-product formation could be reduced by incorporation of the new Asp derivative more efficiently than by introducing the less bulky Asp(OMpe). Significant improvements were observed in cases of prolonged contact with piperidine or DBU. Both beta-carboxy protecting groups were superior to the standard Asp(OtBu) which was also included in this study, but the additional stabilization gained by our new protecting group was valuable especially in syntheses of long peptides or difficult sequences.

3. The aspartimide problem in Fmoc-based SPPS. Part II

M Mergler, F Dick, B Sax, C Stähelin, T Vorherr J Pept Sci. 2003 Aug;9(8):518-26. doi: 10.1002/psc.473.

The sequence dependence of base-catalysed aspartmide formation during Fmoc-based SPPS was systematically studied employing the peptide models H-Val-Lys-Asp-Xaa-Tyr-Ile-OH. The extent of formation of aspartimide and related by-products was determined by RP-HPLC. Considerable amounts of by-products were formed in the case of Xaa = Asp(OtBu), Arg(Pbf), Asn(Mtt), Cys(Acm) and unprotected Thr. Aspartimide formation could be diminished by incorporation of Asp(OMpe) or by employing milder methods for Fmoc cleavage, e.g. hexamethyleneimine/N-methylpyrrolidine/HOBt/NMP/DMSO 4:50:4:71:71 (v/v/w/v/v).