ライフサイエンスコーパス: SPPS

1 SPPS involves the use of excess solvents and reagents wh

2 SPPS protocols, from resin swelling to peptide precipita

3 omophores can be incorporated directly after SPPS via on-resin derivatization of peptides, which is a

4 LPPS combines the advantages of CSPS and SPPS, where peptide elongation is carried out in solutio

5 MF and TFA from peptide synthesis by aqueous SPPS (ASPPS) [Pawlas, J.; Rasmussen, J.

6 , finally unlocking bottlenecks in automated SPPS.

7 o-peptide sequence using standard Fmoc-based SPPS procedures.

8 The technology uses a modified Boc SPPS strategy that avoids the use of anhydrous HF.

9 Avoiding HF extends the scope of Boc SPPS to post-translational modifications that are compat

10 C-peptide was accomplished by optimized Boc-SPPS techniques.

11 is of C-terminal alpha-thioester peptides by SPPS was largely restricted to the use of Boc/Benzyl che

12 also the generality of this newly developed SPPS purification sequence has found application in the

13 only used for removing the Fmoc group during SPPS.

14 heimer's beta-amyloid (Abeta) peptide during SPPS.

15 acid for incorporation into peptides during SPPS.

16 zinonicotinamide ligand into peptides during SPPS.

17 across the entire amino acid sequence during SPPS.

18 SynTag" effectively improves batch- and flow-SPPS of "difficult sequences", enhances the solubility o

19 We introduce the efficient Fmoc-SPPS and peptoid synthesis of Q-proline-based, metal-bin

20 tally stable to conditions required for Fmoc-SPPS.

21 er at a Lys residue epsilon-amine, (ii) Fmoc-SPPS elongation of a desired solubilizing sequence, and

22 the utility of this new protecting group for SPPS and biological experiments.

23 re a protected form of cysteine suitable for SPPS.

24 n innovative four-fragment convergent hybrid SPPS/LPPS strategy combining their individual strengths.

25 thesis (LPPS), and to a lesser extent hybrid SPPS/LPPS, with SPPS emerging as a predominant platform

26 he bicyclic dipeptide Fmoc-ehr=Pro-OH (2) in SPPS or by late-stage oxidation of a precursor peptide a

27 orm for convenient use as building blocks in SPPS.

28 hydrazino acids that can be used directly in SPPS.

29 at are anchored to the solid support used in SPPS.

30 However, the synthesis yield in SPPS often drops drastically for longer amino acid seque

31 This approach involves SPPS on 2-chlorotrityl resin, cyclization of the partial

32 n the broader reliance on inefficient linear SPPS in the field, our work underscores the potential of

33 hesis (SPPS) or by applying a combination of SPPS and ligation approaches to address fundamental ques

34 o examine protein structure in the course of SPPS.

35 ble platform that combines the efficiency of SPPS with the chemical flexibility of a Chemical Process

36 achieving the first gram scale synthesis of SPPS ready C2-O-sLe(X)-Thr-COOH and enabling the scalabl

37 This transformation of SPPS represents a step-change in peptide manufacturing p

38 n a 28-fold yield increase from the original SPPS approach, but also the generality of this newly dev

39 cids which is readily attainable by standard SPPS methodologies.

40 rd amino acids and uses exclusively standard SPPS chemicals or chemicals accessible in one-step synth

41 On average, solid-phase peptide synthesis (SPPS) (PMI ~ 13,000) does not compare favorably with oth

42 of Fmoc-based solid-phase peptide synthesis (SPPS) and beta-hydroxyaspartic acid ligation-mediated pe

43 f traditional Solid Phase Peptide Synthesis (SPPS) and Liquid Phase Peptide Synthesis (LPPS).

44 Solid-phase peptide synthesis (SPPS) and native chemical ligation (NCL) are powerful me

45 scaffold for solid phase peptide synthesis (SPPS) applications when compared to its chlorinated coun

46 elopment of a solid-phase peptide synthesis (SPPS) approach to generate synthetic access to peptide c

47 mpatible with solid-phase peptide synthesis (SPPS) due to the intrinsic acid lability of the P( horiz

48 been used in solid phase peptide synthesis (SPPS) for almost 20 years.

49 ed to support solid phase peptide synthesis (SPPS) for structure-activity studies of the natural prod

50 sal Fmoc/t-Bu solid-phase peptide synthesis (SPPS) has long been intertwined with harmful substances

51 Solid-phase peptide synthesis (SPPS) is a widely used technique in biology and chemistr

52 of biotin and solid phase peptide synthesis (SPPS) of histidine (His)- and human influenza hemaggluti

53 relies on the solid-phase peptide synthesis (SPPS) of N-terminal thioesters (including helix I), in g

54 e prepared by solid-phase peptide synthesis (SPPS) or biosynthetically by protein splicing techniques

55 hesized using solid-phase peptide synthesis (SPPS) or by applying a combination of SPPS and ligation

56 following the solid-phase peptide synthesis (SPPS) protocol and Amyloid beta (39-42) peptide (Boc-Val

57 a process for solid phase peptide synthesis (SPPS) that completely eliminates all solvent intensive w

58 The use of solid-phase peptide synthesis (SPPS) to prepare four such arrays, consisting of 16, 17,

59 : linear Fmoc solid-phase peptide synthesis (SPPS) using several advancements for difficult sequences

60 Solid-phase peptide synthesis (SPPS) using tert-butyloxycarbonyl (Boc)/benzyl (Bzl) che

61 porated after solid-phase peptide synthesis (SPPS) via on-resin derivatization of peptides prepared u

62 orated during solid-phase peptide synthesis (SPPS) with total site specificity.

63 hesis (CSPS), solid-phase peptide synthesis (SPPS), and liquid-phase peptide synthesis (LPPS), have m

64 ing automated solid phase peptide synthesis (SPPS), followed by orthogonal deprotection of the GlcNAc

65 prepared via solid-phase peptide synthesis (SPPS), giving an efficient and modular route to thiopept

66 or Fmoc-based solid-phase peptide synthesis (SPPS), is described.

67 en limited to solid-phase peptide synthesis (SPPS), liquid phase peptide synthesis (LPPS), and to a l

68 of automated solid-phase peptide synthesis (SPPS), many commercial platforms have been developed, fa

69 In solid phase peptide synthesis (SPPS), the most common photoremovable group used for thi

70 Fmoc-strategy solid-phase peptide synthesis (SPPS), was achieved in four steps from delta-gluconolact

71 emi-automated solid-phase peptide synthesis (SPPS), while equipping the antibody with SpyTag.

72 fficient Fmoc solid-phase peptide synthesis (SPPS)-based method for synthesizing disulfide-rich cycli

73 s during Fmoc solid-phase peptide synthesis (SPPS).

74 reaction with solid phase peptide synthesis (SPPS).

75 standard Fmoc solid-phase peptide synthesis (SPPS).

76 ing blocks in solid phase peptide synthesis (SPPS).

77 arbonyl-based solid-phase peptide synthesis (SPPS).

78 direct use in solid phase peptide synthesis (SPPS).

79 o function in Solid-Phase Peptide Synthesis (SPPS).

80 r approach to solid-phase peptide synthesis (SPPS).

81 m amenable to solid-phase peptide synthesis (SPPS).

82 189 utilizing solid-phase peptide synthesis (SPPS).

83 which was selected on the basis of Fmoc-tBu SPPS compatibility and photolysis efficiency.

84 is strategy was documented by evaluating the SPPS of a commercial drug used for prostate and breast c

85 esent work, we describe a new method for the SPPS of C-terminal thioesters using Fmoc/t-Bu chemistry.

86 hitobiosyl-asparagine building block for the SPPS of glycopeptides.

87 Our synthetic approach relies on the SPPS of unprotected epsilon-azido lysine-containing pept

88 ing manuscript add a fourth dimension to the SPPS protecting group scheme.

89 e solid support that are synthesized through SPPS.

90 erous sequences are difficult to prepare via SPPS, and cleaved peptides often have low aqueous solubi

91 nd to a lesser extent hybrid SPPS/LPPS, with SPPS emerging as a predominant platform technology for p