Fmoc-L-1Nal(5-Br,4-OH)-OH

Chemischer Name: N-alpha-(9-Fluorenylmethyloxycarbonyl)-5-bromo-4-hydroxynaphth-1-ylalanine // Synonyme: Fmoc-1Nal(5-Br,4-OH)-OH, (S)-2-((((9H-fluoren-9-yl)methoxy)carbonyl)amino)-3-(5-bromo-4-hydroxynaphthalen-1-yl)propanoic acid

  • Art-Nr.:FAA9070
  • CAS Nr.:3012560-52-7
  • Formel:C28H22BrNO5
  • Lagertemperatur:2-8°C
  • Molare Masse:532,39 g/mol
  • Reinheit:min.95%

Ab 1.330,00 €

Gruppiert Produkte - Artikel
Anzahl Verpackungsgröße Preis SKU Warenverfügbarkeit
100 mg
1.330,00 €
FAA9070.0100
11-20 Arbeitstage
1 g
2.510,00 €
FAA9070.0001
11-20 Arbeitstage
description

This amino acid can be purchased in 50 mg scale as part of a “screening bundle” (see FAS1030). Get in contact for more information. Higher quantities are available on demand.

Non-canonical Amino Acids (ncAAs) enhance the repertoire for building synthetic peptides. Their benefit is that they offer the option to modify the binding characteristics of a given synthetic peptide or protein, and they can affect the susceptibility towards proteolytic degradation. Thus, they may be used to control and enhance potency, stability, specificity, and other important parameters of APIs.

references

Systematic Backbone Conformational Constraints on a Cyclic Melanotropin Ligand Leads to Highly Selective Ligands for Multiple Melanocortin Receptors; M. Cai, U. K. Marelli, J. Bao, J. G. Beck, F. Opperer, F. Rechenmacher, K. R. McLeod, M. R. Zingsheim, L. Doedens, H. Kessler, V. J. Hruby; Journal of Medicinal Chemistry 2015; 58: 6359-6367. https://doi.org/10.1021/acs.jmedchem.5b00102

N-Methylation of Peptides: A New Perspective in Medicinal Chemistry; J. Chatterjee, C. Gilon, A. Hoffman, H. Kessler; Accounts of Chemical Research 2008; 41: 1331-1342. https://doi.org/10.1021/ar8000603

N-Methylation of Peptides and Proteins: An Important Element for Modulating Biological Functions; J. Chatterjee, F. Rechenmacher, H. Kessler; Angewandte Chemie International Edition 2013; 52: 254-269. https://doi.org/10.1002/anie.201205674

Scalable continuous evolution for the generation of diverse enzyme variants encompassing promiscuous activities; G. Rix, E. J. Watkins-Dulaney, P. J. Almhjell, C. E. Boville, F. H. Arnold, C. C. Liu; Nature Communications 2020; 11: 5644. https://doi.org/10.1038/s41467-020-19539-6

Tryptophan-based fluorophores for studying protein conformational changes; P. Talukder, S. Chen, C. T. Liu, E. A. Baldwin, S. J. Benkovic, S. M. Hecht; Bioorganic & Medicinal Chemistry 2014; 22: 5924-5934. https://doi.org/10.1016/j.bmc.2014.09.015

Cyanotryptophans as Novel Fluorescent Probes for Studying Protein Conformational Changes and DNA–Protein Interaction; P. Talukder, S. Chen, B. Roy, P. Yakovchuk, M. M. Spiering, M. P. Alam, M. M. Madathil, C. Bhattacharya, S. J. Benkovic, S. M. Hecht; Biochemistry 2015; 54: 7457-7469. https://doi.org/10.1021/acs.biochem.5b01085

Tryptophan Synthase: Biocatalyst Extraordinaire; E. Watkins-Dulaney, S. Straathof, F. Arnold; Chembiochem: a European journal of chemical biology 2021; 22: 5-16. https://doi.org/10.1002/cbic.202000379


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