751470-47-0

Usage

Uses

Used in Peptide and Protein Synthesis:
Fmoc-L-cysteic acid is used as a building block for the synthesis of peptides and proteins, due to its ability to protect the amino group during the synthesis process. The Fmoc protecting group can be selectively removed, allowing for the stepwise assembly of peptide chains in solid-phase peptide synthesis.
Used in Biochemistry Research:
Fmoc-L-cysteic acid is used as a research tool for studying the properties and functions of peptides and proteins. Its ability to modify the properties of these biomolecules makes it instrumental in understanding their structure-function relationships and exploring their potential applications in various biological processes.
Used in Pharmaceutical Development:
Fmoc-L-cysteic acid is used as a key component in the development of pharmaceuticals, particularly in the design and synthesis of bioactive peptides and proteins with therapeutic potential. Its role in peptide synthesis and property modification enables the creation of novel drug candidates with specific biological activities.
Used in Chemical Modification of Biomolecules:
Fmoc-L-cysteic acid is used as a modifying agent for the alteration of the properties of peptides and proteins. This modification can enhance their stability, solubility, or biological activity, making them more suitable for various applications, such as drug delivery or targeted therapies.

Upstream product

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Relevant academic research and scientific papers

A trimethyllysine-containing trityl tag for solubilizing hydrophobic peptides

Hydrophobic membrane peptides/proteins having low water solubility are often difficult to prepare. To overcome this issue, temporal introduction of solubilizing tags has been demonstrated to be beneficial. Following our recent work on the solubilization of a difficult target by using a hydrophilic oligo-Lys tag bearing a trityl linker (Trt-K method), this paper describes a comparative study of the solubilizing abilities of several peptidic trityl tags containing Lys, Arg, Glu, Asn, N?-tri-Me-Lys or Cys-sulfonate using two hydrophobic model peptides. Among the tags evaluated, that containing N?-tri-Me-Lys exhibits superior solubilizing ability.

Photoactivatable Rhodamine Spiroamides and Diazoketones Decorated with "universal Hydrophilizer" or Hydroxyl Groups

Photoactivatable rhodamine spiroamides and spirocyclic diazoketones emerged recently as synthetic markers applicable in multicolor super-resolution microscopy. However, their applicability in single molecule localization microscopy (SMLM) is often limited by aggregation, unspecific adhesion, and low reactivity caused by insufficient solubility and precipitation from aqueous solutions. We report here two synthetic modifications increasing the polarity of compact polycyclic and hydrophobic labels decorated with a reactive group: attachment of 3-sulfo-l-alanyl-beta-alanine dipeptide (a "universal hydrophilizer") or allylic hydroxylation in photosensitive rhodamine diazoketones (and spiroamides). The super-resolution images of tubulin and keratin filaments in fixed and living cells exemplify the performance of "blinking" spiroamides derived from N,N,N′,N′-tetramethyl rhodamine.

DELIVERY SYSTEMS FOR CONTROLLED DRUG RELEASE

The present invention provides a compound having the structure of Formula (I) or a pharmaceutically acceptable salt, hydrate, solvate, or isomer thereof, for the controlled delivery and release of Agent.

Functional group requirements within the peptide H-Pro-Pro-Asp-NH2 as a catalyst for aldol reactions

H-Pro-Pro-Asp-NH2 1 is a versatile catalyst for asymmetric aldol reactions. In this work, the functional group tolerance within the catalyst structure has been examined. Several analogs of H-Pro-Pro-Asp-NH2 in which the N-terminal secondary amine or the carboxylic acid in the side chain of the aspartic acid residue is replaced by different functional groups were prepared. Evaluation of their catalytic properties revealed that both the N-terminal secondary amine and the carboxylic acid are important for catalysis. The implications for the reaction mechanism are discussed.