Innovative Tools for Molecular and Cell Biology

Innovative Tools for Molecular and Cell Biology

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Amino Acids Derivatives for Solid-Phase Peptide Synthesis

Fmoc and Boc-Protected Amino Acids

Fmoc Amino Acids

Fmoc Amino Acids - Lab-Proven Quality

Features

  • Fmoc and Boc are the most common alpha-amino-protecting groups for solid-phase peptide synthesis
  • Standard amino acids derivatives
  • Fmoc/Boc-amino acid cartridges
  • Synthesis reagents, resins & accessories
  • Unusual amino acids derivatives
  • All products are manufactured according to ISO 9001 guidelines

Description

  • Fmoc (9-fluorenylmethoxy-carbonyl) and Boc (tert-butyloxycarbonyl) based solid phase peptide synthesis (SPPS) are preferred coupling strategies for many researchers due to the versatility, ease of use, and mild deprotection conditions. The importance of peptides in basic research and medicine make SPPS an essential technique for building the necessary tools for studying anything from peptide structure and folding, to complex peptide/protein-biomolecule interactions.

  • Peptides are synthesized by coupling the carboxyl group or C-terminus of one amino acid to the amino group or N-terminus of another. Due to the possibility of unintended reactions, protecting groups are usually necessary.
  • The general principle of SPPS is one of repeated cycles of deprotection-wash-coupling-wash. The free N-terminal amine of a solid-phase attached peptide is coupled to a single N-protected amino acid unit. This unit is then deprotected, revealing a new N-terminal amine to which a further amino acid may be attached.
  • There are two majorly used forms of SPPS – Fmoc and Boc. Unlike ribosome protein synthesis, solid-phase peptide synthesis proceeds in a C-terminal to N-terminal fashion. The N-termini of amino acid monomers is protected by either of these two groups and added onto a deprotected amino acid chain.
  • The Boc group is covalently bound to the amino group to suppress its nucleophilicity. The C-terminal amino acid is covalently linked to the resin through a linker. Next, the Boc group is removed with acid, such as trifluoroacetic acid (TFA). This forms a positively charged amino group, which is neutralized and coupled to the incoming activated amino acid.
  • The Fmoc method allows for a milder deprotection scheme. This method utilizes a base, usually piperidine (20–50%) in DMF in order to remove the Fmoc group to expose the α-amino group for reaction with an incoming activated amino acid. Unlike the acid used to deprotect the α-amino group in Boc methods, Fmoc SPPS uses a base, and thus the exposed amine is neutral. Therefore, no neutralization of the peptide-resin is required. Because the liberated fluorenyl group is a chromophore, deprotection by Fmoc can be monitored by UV absorbance of the runoff, a strategy which is employed in automated synthesizers.

ORDER INFORMATION

  • For shipping and storage information please click on Order#.
  • Standard Amino Acids
Order# Description Amount Price Data Sheet
20121AS Fmoc-Ala-OH 100 g 120,00 PDF
20141AS Fmoc-Arg(Pbf)-OH 100 g 1089,00 PDF
20123AS Fmoc-Asn(Trt)-OH 100 g 311,00 PDF
20124AS Fmoc-Asp(OtBu)-OH 100 g 311,00 PDF
20125AS Fmoc-Cys(Trt)-OH 100 g 311,00 PDF
20127AS Fmoc-Gln(Trt)-OH 100 g 311,00 PDF
20126AS Fmoc-Glu(OtBu)-OH 100 g 311,00 PDF
20128AS Fmoc-Gly-OH 100 g 120,00 PDF
20129AS Fmoc-His(Trt)-OH 100 g 311,00 PDF
20130AS Fmoc-Ile-OH 100 g 120,00 PDF
20131AS Fmoc-Leu-OH 100 g 120,00 PDF
20132AS Fmoc-Lys(Boc)-OH 100 g 311,00 PDF
20133AS Fmoc-Met-OH 100 g 120,00 PDF
20134AS Fmoc-Phe-OH 100 g 120,00 PDF
20135AS Fmoc-Pro-OH 100 g 120,00 PDF
20136AS Fmoc-Ser(tBu)-OH 100 g 311,00 PDF
20137AS Fmoc-Thr(tBu)-OH 100 g 311,00 PDF
25200AS Fmoc-Trp(Boc)-OH 100 g 820,00 PDF
20139AS Fmoc-Tyr(tBu)-OH 100 g 311,00 PDF
20140AS Fmoc-Val-OH 100 g 120,00 PDF
20829AS Boc-Cys(Trt)-OH 100 g 622,00 PDF
20869AS Boc-Gly-OH 100 g 107,00 PDF
20875AS Boc-His(Bom)-OH 100 g 1400,00 PDF
20902AS Boc-Trp-OH 100 g 170,00 PDF