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1 omophores can be incorporated directly after SPPS via on-resin derivatization of peptides, which is a
2 o-peptide sequence using standard Fmoc-based SPPS procedures.
3           The technology uses a modified Boc SPPS strategy that avoids the use of anhydrous HF.
4         Avoiding HF extends the scope of Boc SPPS to post-translational modifications that are compat
5  C-peptide was accomplished by optimized Boc-SPPS techniques.
6 is of C-terminal alpha-thioester peptides by SPPS was largely restricted to the use of Boc/Benzyl che
7 only used for removing the Fmoc group during SPPS.
8 heimer's beta-amyloid (Abeta) peptide during SPPS.
9  acid for incorporation into peptides during SPPS.
10 zinonicotinamide ligand into peptides during SPPS.
11 across the entire amino acid sequence during SPPS.
12 tally stable to conditions required for Fmoc-SPPS.
13 er at a Lys residue epsilon-amine, (ii) Fmoc-SPPS elongation of a desired solubilizing sequence, and
14 orm for convenient use as building blocks in SPPS.
15 at are anchored to the solid support used in SPPS.
16              However, the synthesis yield in SPPS often drops drastically for longer amino acid seque
17                       This approach involves SPPS on 2-chlorotrityl resin, cyclization of the partial
18 o examine protein structure in the course of SPPS.
19 mpatible with solid-phase peptide synthesis (SPPS) due to the intrinsic acid lability of the P( horiz
20  been used in solid phase peptide synthesis (SPPS) for almost 20 years.
21 ed to support solid phase peptide synthesis (SPPS) for structure-activity studies of the natural prod
22               Solid-phase peptide synthesis (SPPS) is a widely used technique in biology and chemistr
23 relies on the solid-phase peptide synthesis (SPPS) of N-terminal thioesters (including helix I), in g
24 e prepared by solid-phase peptide synthesis (SPPS) or biosynthetically by protein splicing techniques
25 following the solid-phase peptide synthesis (SPPS) protocol and Amyloid beta (39-42) peptide (Boc-Val
26    The use of solid-phase peptide synthesis (SPPS) to prepare four such arrays, consisting of 16, 17,
27               Solid-phase peptide synthesis (SPPS) using tert-butyloxycarbonyl (Boc)/benzyl (Bzl) che
28 porated after solid-phase peptide synthesis (SPPS) via on-resin derivatization of peptides prepared u
29 orated during solid-phase peptide synthesis (SPPS) with total site specificity.
30 ing automated solid phase peptide synthesis (SPPS), followed by orthogonal deprotection of the GlcNAc
31  prepared via solid-phase peptide synthesis (SPPS), giving an efficient and modular route to thiopept
32 or Fmoc-based solid-phase peptide synthesis (SPPS), is described.
33 Fmoc-strategy solid-phase peptide synthesis (SPPS), was achieved in four steps from delta-gluconolact
34 emi-automated solid-phase peptide synthesis (SPPS), while equipping the antibody with SpyTag.
35 fficient Fmoc solid-phase peptide synthesis (SPPS)-based method for synthesizing disulfide-rich cycli
36 standard Fmoc solid-phase peptide synthesis (SPPS).
37 ing blocks in solid phase peptide synthesis (SPPS).
38 arbonyl-based solid-phase peptide synthesis (SPPS).
39 reaction with solid phase peptide synthesis (SPPS).
40  which was selected on the basis of Fmoc-tBu SPPS compatibility and photolysis efficiency.
41 esent work, we describe a new method for the SPPS of C-terminal thioesters using Fmoc/t-Bu chemistry.
42 hitobiosyl-asparagine building block for the SPPS of glycopeptides.
43         Our synthetic approach relies on the SPPS of unprotected epsilon-azido lysine-containing pept
44 e solid support that are synthesized through SPPS.

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