96383-44-7

Basic information

• Product Name: FMOC-L-SER(BETA-D-GALAC4)-OH
• Synonyms: GALACTOSYLATED L-SERINE;FMOC-L-SER(BETA-D-GALAC4)-OH;N-FMOC-O-(2,3,4,6-TETRA-O-ACETYL-BETA-D-GALACTOPYRANOSYL)-L-SERINE;N-ALPHA-(9-FLUORENYLMETHYLOXYCARBONYL)-O-(2,3,4,6-TETRA-O-ACETYL-BETA-D-GALACTOPYRANOSYL)-L-SERINE;Fmoc-L-Ser(β-D-Gal(Ac)4)-OH;N-[(9H-Fluoren-9-ylmethoxy)carbonyl]-O-(2,3,4,6-tetra-O-acetyl-beta-D-galactopyranosyl)-L-serine
• CAS NO: 96383-44-7
• Molecular Formula: C₃₂H₃₅NO₁₄
• Molecular Weight: 657.62
• Product Categories: Glycoamino Acid
• Mol File: 96383-44-7.mol
• Article Data: 12

Chemical Properties

• Appearance: /
• Storage Temp.: -20°C
• CAS DataBase Reference: FMOC-L-SER(BETA-D-GALAC4)-OH(CAS DataBase Reference)
• NIST Chemistry Reference: FMOC-L-SER(BETA-D-GALAC4)-OH(96383-44-7)
• EPA Substance Registry System: FMOC-L-SER(BETA-D-GALAC4)-OH(96383-44-7)

Safety Data

• WGK Germany: 3
• Hazardous Substances Data: 96383-44-7(Hazardous Substances Data)

Usage

General Description

FMOC-L-SER(BETA-D-GALAC4)-OH, also known as FMOC-L-serine-β-D-galactoside, is a chemical compound that consists of an FMOC-protected serine residue linked to a β-D-galactoside moiety. It is commonly used in the field of organic chemistry as a building block for the synthesis of glycopeptides and glycoproteins. The FMOC group provides protection for the serine residue during chemical reactions, while the β-D-galactoside moiety imparts specific biological and structural properties to the molecule. FMOC-L-SER(BETA-D-GALAC4)-OH has applications in the study of carbohydrate-protein interactions, drug development, and the creation of biomimetic materials.

Upstream product

• 73724-45-5 N-(9H-fluoren-9-ylmethoxycarbonyl)-L-serine 
• 4163-60-4 β-D-galactose peracetate 
• 25878-60-8 D-galactose pentaacetate 
• 70191-05-8 2,3,4,6-tetra-O-acetyl-β-D-galactopyranose 
• 3068-32-4 1-bromo-1-deoxy-2,3,4,6-tetra-O-acetyl-a-D-galactopyranoside 
• 136497-85-3 2-(9H-Fluoren-9-ylmethoxycarbonylamino)-3-hydroxy-propionic acid allyl ester 

Downstream Products

• 350689-32-6 3-O-(2,3,4,6-tetra-O-acetyl-β-D-galactopyranosyl)-N-(diphenoxyphosphoryl)-L-serine tetradecanamide 

Relevant articles and documents

How post-translational modifications influence amyloid formation: A systematic study of phosphorylation and glycosylation in model peptides

A reciprocal relationship between phosphorylation and O-glycosylation has been reported for many cellular processes and human diseases. The accumulated evidence points to the significant role these post-translational modifications play in aggregation and fibril formation. Simplified peptide model systems provide a means for investigating the molecular changes associated with protein aggregation. In this study, by using an amyloid-forming model peptide, we show that phosphorylation and glycosylation can affect folding and aggregation kinetics differently. Incorporation of phosphoserines, regardless of their quantity and position, turned out to be most efficient in preventing amyloid formation, whereas O-glycosylation has a more subtle effect. The introduction of a single βgalactose does not change the folding behavior of the model peptide, but does alter the aggregation kinetics in a site-specific manner. The presence of multiple galactose residues has an effect similar to that of phosphorylation.

Effects of Glycosylation and d -Amino Acid Substitution on the Antitumor and Antibacterial Activities of Bee Venom Peptide HYL

Glycosylation is a promising strategy for modulating the physicochemical properties of peptides. However, the influence of glycosylation on the biological activities of peptides remains unknown. Here, we chose the bee venom peptide HYL as a model peptide and 12 different monosaccharides as model sugars to study the effects of glycosylation site, number, and monosaccharide structure on the biochemical properties, activities, and cellular selectivities of HYL derivatives. Some analogues of HYL showed improvement not only in cell selectivity and proteolytic stability but also in antitumor and antimicrobial activity. Moreover, we found that the helicity of glycopeptides can affect its antitumor activity and proteolytic stability, and the α-linked d-monosaccharides can effectively improve the antitumor activity of HYL. Therefore, it is possible to design peptides with improved properties by varying the number, structure, and position of monosaccharides. What's more, the glycopeptides HYL-31 and HYL-33 show a promising prospect for antitumor and antimicrobial drugs development, respectively. In addition, we found that the d-lysine substitution strategy can significantly improve the proteolytic stability of HYL. Our new approach provides a reference or guidance for the research of novel antitumor and antimicrobial peptide drugs.

Carbohydrate-π interactions: What are they worth?

Protein-carbohydrate interactions play an important role in many biologically important processes. The recognition is mediated by a number of noncovalent interactions, including an interaction between the α-face of the carbohydrate and the aromatic side chain of the protein. To elucidate this interaction, it has been studied in the context of a β-hairpin in aqueous solution, in which the interaction can be investigated in the absence of other cooperative noncovalent interactions. In this β-hairpin system, both the aromatic side chain and the carbohydrate were varied in an effort to gain greater insight into the driving force and magnitude of the carbohydrate-π interaction. The magnitude of the interaction was found to vary from -0.5 to -0.8 kcal/mol, depending on the nature of the aromatic ring and the carbohydrate. Replacement of the aromatic ring with an aliphatic group resulted in a decrease in interaction energy to -0.1 kcal/mol, providing evidence for the contribution of CH-π interactions to the driving force. These findings demonstrate the significance of carbohydrate-π interactions within biological systems and also their utility as a molecular recognition element in designed systems.