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Fmoc-L-Ala(BCP-OBz)-OH

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

Category

Bicyclic Amino Acids

Catalog number

BAT-000773

Molecular Formula

C30H27NO6

Molecular Weight

497.54

Synonyms

N-alpha-(9-Fluorenylmethyloxycarbonyl)-3-(3-benzoyloxybicyclo[1.1.1]pentan-1-yl)-L-alanine; Fmoc-Ala(BCP-OBz); (S)-2-(((9H-fluoren-9-yl)methoxy)carbonylamino)-3-(3-(benzoyloxy)bicyclo[1.1.1]pentan-1-yl)propanoic acid

Storage

Store at 2-8 °C

Fmoc-L-Ala(BCP-OBz)-OH, a derivative of protected amino acid, finds primary utility in peptide synthesis. Here are the key applications of Fmoc-L-Ala(BCP-OBz)-OH presented with high perplexity and burstiness:

Peptide Synthesis: Serving as a foundational component in solid-phase peptide synthesis (SPPS), Fmoc-L-Ala(BCP-OBz)-OH plays a pivotal role in constructing custom peptides for various research and therapeutic applications. The Fmoc (Fluorenylmethyloxycarbonyl) group attached to this compound allows for effortless removal under mildly basic conditions facilitating the sequential elongation of peptides. This process is essential for the tailored creation of peptides with specific functionalities.

Pharmacological Research: Peptides synthesized utilizing Fmoc-L-Ala(BCP-OBz)-OH serve as essential tools in exploring drug interactions and probing protein function.s These peptides function as valuable probes for studying receptor binding enzyme activity and protein-protein interactions. Understanding the intricate interplay between these molecular components is critical for advancing pharmaceutical development and refining therapeutic approaches.

Biochemical Studies: In the realm of biochemical research, peptides derived from Fmoc-L-Ala(BCP-OBz)-OH aid in unraveling the structure and function of proteins. Researchers leverage these peptides to mimic specific protein segments enabling investigations into protein folding stability and interactions. Such in-depth studies yield crucial insights into disease mechanisms and inform the development of targeted therapeutic interventions for complex medical conditions.

Antibody Production: Custom peptides generated through the utilization of Fmoc-L-Ala(BCP-OBz)-OH serve as potent antigens for the production of specialized antibodies. These antibodies play a vital role in detecting proteins in diverse assays like Western blotting ELISA and immunohistochemistry. This application proves invaluable in diagnostic procedures therapeutic monitoring and fundamental scientific research endeavors offering a comprehensive approach to studying protein interactions and function.

1. Ammodendrine and N-methylammodendrine enantiomers: isolation, optical rotation, and toxicity

Stephen T Lee, Russell J Molyneux, Kip E Panter, Cheng-Wei Tom Chang, Dale R Gardner, James A Pfister, Massoud Garrossian J Nat Prod. 2005 May;68(5):681-5. doi: 10.1021/np0580199.

Ammodendrine (1) was found to occur as a mixture of enantiomers in two different collections of plants identified as Lupinus formosus. The ammodendrine fraction was reacted in a peptide coupling reaction with 9-fluorenylmethoxycarbonyl-L-alanine (Fmoc-L-Ala-OH) to give diastereomers, which were separated by preparative HPLC. The pure D- and L-ammodendrine enantiomers were then obtained by Edman degradation. Optical rotation measurements revealed that the D- and L-enantiomers had optical rotations of [alpha]24D +5.4 and -5.7, respectively. D- and L-N-methylammodendrine enantiomers were synthesized from the corresponding ammodendrine enantiomers, and their optical rotations established as [alpha]23D +62.4 and -59.0, respectively. A mouse bioassay was used to determine the difference in toxicity between these two pairs of naturally occurring enantiomers. The LD50 of (+)-D-ammodendrine in mice was determined to be 94.1 +/- 7 mg/kg and that of (-)-L-ammodendrine as 115.0 +/- 7 mg/kg. The LD50 of (+)-D-N-methylammodendrine in mice was estimated to be 56.3 mg/kg, while that of (-)-L-N-methylammodendrine was determined to be 63.4 +/- 5 mg/kg. These results establish the rotation values for pure ammodendrine and N-methylammodendrine and indicate that there is little difference in acute murine toxicity between the respective enantiomers.

2. Relative toxicities and neuromuscular nicotinic receptor agonistic potencies of anabasine enantiomers and anabaseine

Stephen T Lee, Kristin Wildeboer, Kip E Panter, William R Kem, Dale R Gardner, Russell J Molyneux, Cheng-Wei Tom Chang, Ferenc Soti, James A Pfister Neurotoxicol Teratol. 2006 Mar-Apr;28(2):220-8. doi: 10.1016/j.ntt.2005.12.010. Epub 2006 Feb 20.

Anabasine occurring in wild tree tobacco (Nicotiana glauca) and anabaseine occurring in certain animal venoms are nicotinic receptor agonist toxins. Anabasine lacks the imine double bond of anabaseine; the two possible enantiomers of anabasine occur in N. glauca. A comparision of the relative potencies of S- and R-anabasine has not been previously reported. We separated the enantiomers of anabasine by reaction of the racemic N. glauca natural product with 9-fluorenylmethoxycarbonyl-L-alanine (Fmoc-L-Ala-OH) to give diastereomers, which were separated by preparative reversed phase HPLC. The S- and R-anabasine enantiomer fractions were then obtained by Edman degradation. A mouse bioassay was used to determine the relative lethalities of S- and R-enriched anabasine enantiomers. The intravenous LD50 of the (+)-R-anabasine rich fraction was 11 +/- 1.0 mg/kg and that of the (-)-S-anabasine-rich fraction was 16 +/- 1.0 mg/kg. The LD50 of anabaseine was 0.58 +/- 0.05 mg/kg. Anabaseine was significantly more toxic in the mouse bioassay than S-anabasine (27-fold) and R-anabasine (18-fold). The relative agonistic potencies of these three alkaloids on human fetal nicotinic neuromuscular receptors were of the same rank order: anabaseine>>R-anabasine>S-anabasine.