856412-22-1

Basic information

• Product Name: (S)-N-Fmoc-2-(4'-pentenyl)glycine
• Synonyms: (S)-N-Fmoc-2-(4'-pentenyl)glycine;(2S)-2-[[(9H-Fluoren-9-ylmethoxy)carbonyl]amino]-6-heptenoic acid;N-Fmoc-(S)-2-aminohept-6-enoic acid;(S)-2-((((9H-Fluoren-9-yl)Methoxy)carbonyl)aMino)hept-6-enoic acid;(2S)-2-(Fmoc-amino)-6-heptenoic acid
• CAS NO: 856412-22-1
• Molecular Formula: C₂₂H₂₃NO₄
• Molecular Weight: 365
• EINECS: -0
• Mol File: 856412-22-1.mol

Chemical Properties

• Boiling Point: 589.7±45.0 °C at 760 mmHg
• Flash Point: 310.5±28.7 °C
• Appearance: /
• Density: 1.202
• Storage Temp.: 2-8°C
• PKA: 3.87±0.21(Predicted)
• CAS DataBase Reference: (S)-N-Fmoc-2-(4'-pentenyl)glycine(CAS DataBase Reference)
• NIST Chemistry Reference: (S)-N-Fmoc-2-(4'-pentenyl)glycine(856412-22-1)
• EPA Substance Registry System: (S)-N-Fmoc-2-(4'-pentenyl)glycine(856412-22-1)

Safety Data

• Hazardous Substances Data: 856412-22-1(Hazardous Substances Data)

Usage

Uses

Used in Organic Chemistry:
(S)-N-Fmoc-2-(4'-pentenyl)glycine is used as a building block for the synthesis of complex organic molecules, leveraging its unique structure and reactivity to facilitate the creation of novel compounds with potential applications in various fields.
Used in Biochemistry:
In biochemistry, (S)-N-Fmoc-2-(4'-pentenyl)glycine is used as a component in peptide synthesis, where the Fmoc protecting group allows for the stepwise assembly of peptide chains. (S)-N-Fmoc-2-(4'-pentenyl)glycine contributes to the development of new peptide-based drugs and the study of protein structure and function.
Used in Pharmaceutical Industry:
(S)-N-Fmoc-2-(4'-pentenyl)glycine is used as a key intermediate in the synthesis of pharmaceutical compounds, particularly for the development of peptide-based drugs. Its unique properties enable the design and synthesis of molecules with specific biological activities, potentially leading to the discovery of new therapeutic agents.
Used in Research and Development:
In research and development, (S)-N-Fmoc-2-(4'-pentenyl)glycine is employed as a valuable tool for studying biological processes and exploring the potential of novel molecular constructs. Its unique structure allows researchers to investigate the effects of specific modifications on peptide and protein properties, contributing to a deeper understanding of molecular interactions and functions.

Upstream product

• 82911-69-1 N-(9H-fluoren-2-ylmethoxycarbonyloxy)succinimide 
• 166734-64-1 (S)-2-amino-hept-6-enoic acid 
• 1319191-90-6 (S)-2-amino-N-((1R,2R)-1-hydroxy-1-phenylpropan-2-yl)-N-methylhept-6-enamide 
• 28920-43-6 (fluorenylmethoxy)carbonyl chloride 
• 1119-51-3 bromopentene 
• 204711-96-6 (2S)-2-[(tert-butoxycarbonyl)amino]-6-heptenoic acid methyl ester 
• 89985-87-5 methyl (2S)-2-tert-butoxycarbonylamino-4-pentenoate 
• 89895-48-7 C₇H₁₃NO₂*ClH 
• 7766-48-5 1-iodo-4-pentene 
• 102774-86-7 9-fluorenylmethyl N-succinimidyl carbonate 

Relevant articles and documents

Mono-Substituted Hydrocarbon Diastereomer Combinations Reveal Stapled Peptides with High Structural Fidelity

Modified peptides, such as stapled peptides, which replicate the structure of α-helical protein segments, represent a potential therapeutic advance. However, the 3D solution structure of these stapled peptides is rarely explored beyond the acquisition of circular dichroism (CD) data to quantify bulk peptide helicity; the detailed backbone structure, which underlies this, is typically undefined. Diastereomeric stapled peptides based on helical sections of three proteins (αSyn, Cks1 and CK1α) were generated; their overall helicity was quantified by CD; and the most helical peptide from each series was selected for structural analysis. Solution-phase models for the optimised peptides were generated using NMR-derived restraints and a modified CHARMM22 force field. Comparing these models with PDB structures allowed deviation between the stapled peptides and critical helical regions to be evaluated. These studies demonstrate that CD alone is not sufficient to assess the structural fidelity of a stapled peptide.

Reversibly switching the conformation of short peptide through in-tether chiral sulfonium auxiliary

A chirality induced helicity method has been developed to modulate the peptide's biophysical and biochemical properties. We report herein a novel approach for reversibly switching the conformation of short constraint α-helical peptides through alkylation of the in-tether thioether and dealkylation of the chiral sulfonium. This traceless redox sensitive tagging strategy broadened our scope of CIH (chirality induced helicity) strategy and provided a valuable approach to functionalize the peptide tether.

Improved synthesis of unnatural amino acids for peptide stapling

The procedures for the synthesis of various α-alkenyl and alkyne amino acids were systematically optimized in light of enhancing atom economy, reducing hazardous reagent usage, and simplifying workup. By starting with Boc-Pro-OH and coupling with EDCI/DMAP followed by alkylation, chiral auxiliary was synthesized with high yield and enantioselectivity. For alkylation of the chiral complex, tBuONa was found and proved by quantitative calculation to be superior to tBuOK in generating more nucleophilic enolate salt, thereby can significantly enhance yield under room temperature. Final Fmoc protection was also dramatically facilitated in one-pot sequential manner by adding EDTA-2Na as the nickel chelator. Synthesis of α-bisalkenyl amino acid was also accomplished by achiral complex approach with high yield and efficacy. Accordingly, five most commonly used N-Fmoc protected α-alkenyl and alkynyl amino acids were synthesized and characterized.

An in-tether sulfilimine chiral center induces helicity in short peptides

A precisely positioned sulfilimine chiral center in the tether of a stabilized peptide would determine the peptide's secondary structure. Peptide sulfilimines could be prepared by a facile chloramine T oxidation and the two resulting peptide diastereomers showed significant differences in their secondary structures, which were supported by circular dichroism spectroscopy and NMR.

Insight into Transannular Cyclization Reactions to Synthesize Azabicyclo[X.Y.Z]alkanone Amino Acid Derivatives from 8-, 9-, and 10-Membered Macrocyclic Dipeptide Lactams

An efficient method for synthesizing different functionalized azabicyclo[X.Y.0]alkanone amino acid derivatives has been developed employing electrophilic transannular cyclizations of 8-, 9-, and 10-membered unsaturated macrocycles to form 5,5-, 6,5-, 7,5-, and 6,6-fused bicylic amino acids, respectively. Macrocycles were obtained by a sequence featuring peptide coupling of vinyl-, allyl-, homoallyl-, and homohomoallylglycine building blocks followed by ring-closing metathesis. X-ray crystallographic analyses of the 8-, 9-, and 10-membered macrocyclic lactam starting materials as well as certain bicyclic amino acid products provided insight into their conformational preferences as well as the mechanism for the diastereoselective formation of specific azabicycloalkanone amino acids by way of transannular iodolactamization reactions. (Chemical Equation Presented).

Influence of α-methylation in constructing stapled peptides with olefin metathesis

Ring-closing metathesis is commonly utilized in peptide macro-cyclization. The influence of α-methylation of the amino acids bearing the olefin moieties has never been systematically studied. In this report, controlled reactions unambiguously indicate that α-methylation at the N-terminus of the metathesis sites is crucial for this reaction to occur. Also, we first elucidated that the E-isomers of stapled peptides are significantly more helical than the Z-isomers.

Robust asymmetric synthesis of unnatural alkenyl amino acids for conformationally constrained α-helix peptides

The efficient asymmetric synthesis of unnatural alkenyl amino acids required for peptide 'stapling' has been achieved using alkylation of a fluorine-modified NiII Schiff base complex as the key step.

Monosubstituted alkenyl amino acids for peptide "stapling"

Alkenylglycine amino acids were assessed as potential candidates for hydrocarbon stapling and shown to be effective in stapling of the BID BH3 peptide.

NUCLEIC ACID BINDING COMPOUNDS, METHODS OF MAKING, AND USE THEREOF

The present invention relates to oligomer compounds, including dimers and trimers, formed by a disulfide, sulfinyl thio, olefin or hydrocarbon bond, or a hydrazone exchange bond between two or more monomers. Methods of making the monomers and the oligomers is also disclosed. Use of the compounds for inhibiting the activity of target RNA molecules, particularly those having a secondary structure that include a stem or stem-loop formation. Dimer compounds capable of inhibiting the activity of an HIV-1 RNA frameshifting stem-loop and a (CUG)n expanded repeat stem- loop are disclosed, as are methods of treating diseases associated with these target RNA molecules.

Bridged β3-Peptide Inhibitors of p53-hDM2 complexation: Correlation between affinity and cell permeability

Abstract: (Figure Presented) β-peptides possess several features that are desirable in peptidomimetics; they are easily synthesized, fold into stable secondary structures in physiologic buffers, and resist proteolysis. They can also bind to a diverse array of proteins to inhibit their interactions with α-helical ligands. β-peptides are usually not cell-permeable, however, and this feature limits their utility as research tools and potential therapeutics. Appending an Arg8 sequence to a β-peptide improves uptake but adds considerable mass. We previously reported that embedding a small cationic patch within a PPII, α-, or β-peptide helix improves uptake without the addition of significant mass. In another mass-neutral strategy, Verdine, Walensky, and others have reported that insertion of a hydrocarbon bridge between the i and i + 4 positions of an α-helix also increases cell uptake. Here we describe a series of β-peptides containing diether and hydrocarbon bridges and compare them on the basis of cell uptake and localization, affinities for hDM2, and 14-helix structure. Our results highlight the relative merits of the cationic-patch and hydrophobic-bridge strategies for improving β-peptide uptake and identify a surprising correlation between uptake efficiency and hDM2 affinity. Copyright