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  2. Fluorenylmethyloxycarbonyl protecting group - Wikipedia

    en.wikipedia.org/wiki/Fluorenylmethyloxycarbonyl...

    The fluorenylmethoxycarbonyl protecting group (Fmoc) is a base-labile amine protecting group used in organic synthesis, particularly in peptide synthesis [1]. It is popular for its stability toward acids and hydrolysis and its selective removal by weak bases, such as piperidine , without affecting most other protecting groups or sensitive ...

  3. Peptide synthesis - Wikipedia

    en.wikipedia.org/wiki/Peptide_synthesis

    In organic chemistry, peptide synthesis is the production of peptides, compounds where multiple amino acids are linked via amide bonds, also known as peptide bonds. Peptides are chemically synthesized by the condensation reaction of the carboxyl group of one amino acid to the amino group of another.

  4. Protecting group - Wikipedia

    en.wikipedia.org/wiki/Protecting_group

    The technique was introduced in the field of peptide synthesis by Robert Bruce Merrifield in 1977. [111] For peptide synthesis via automated machine, the orthogonality of the Fmoc group (basic cleavage), the tert‑butyl group (acidic cleavage) and diverse protecting groups for functional groups on the amino acid side-chains are used. [112]

  5. Pseudoproline - Wikipedia

    en.wikipedia.org/wiki/Pseudoproline

    The chemical synthesis of large peptides is still limited by problems of low solvation during solid phase peptide synthesis (SPPS) or limited solubility of fully protected peptide fragments: even chemoselective ligation methods are hampered by self-association of unprotected peptide blocks.

  6. Solid-phase synthesis - Wikipedia

    en.wikipedia.org/wiki/Solid-phase_synthesis

    The process was originally developed in the 1950s and 1960s by Robert Bruce Merrifield in order to synthesise peptide chains, [4] and which was the basis for his 1984 Nobel Prize in Chemistry. [5] In the basic method of solid-phase synthesis, building blocks that have two functional groups are used.

  7. Native chemical ligation - Wikipedia

    en.wikipedia.org/wiki/Native_chemical_ligation

    Fmoc chemistry solid phase peptide synthesis techniques for generating peptide-thioesters are based on the synthesis of peptide hydrazides that are converted to peptide thioesters post-synthetically. Polypeptide C-terminal thioesters can also be produced in situ , using so-called N,S -acyl shift systems.

  8. Fluorenylmethyloxycarbonyl chloride - Wikipedia

    en.wikipedia.org/wiki/Fluorenylmethyloxycarbonyl...

    Fluorenylmethyloxycarbonyl chloride (Fmoc-Cl) is a chloroformate ester. It is used to introduce the fluorenylmethyloxycarbonyl protecting group as the Fmoc carbamate . Preparation

  9. DEPBT - Wikipedia

    en.wikipedia.org/wiki/DEPBT

    DEPBT (3-(diethoxyphosphoryloxy)-1,2,3-benzotriazin-4(3H)-one) is a peptide coupling reagent used in peptide synthesis.It shows remarkable resistance to racemization. [1]Fmoc-Dab(Mtt)-OH, a commercially available amino acid building block for solid-phase peptide synthesis (SPPS), was proven to undergo rapid lactamization, instead of reacting with the N-terminal end of the peptide.

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