Application of Dmb-Dipeptides in the Fmoc SPPS of Difficult and Aspartimide-Prone Sequences

Cardona, Valérie; Eberle, I.; Barthelemy, Sophie; Beythien, Joerg; Doerner, B.; Schneeberger, P.; Keyte, John W.; White, Peter

doi:10.1007/s10989-008-9154-z

Cited by 57 publications

(60 citation statements)

References 20 publications

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“…Along this line, the MUB 70 sequence accumulates eight highly sensitive occurrences (three Asp-Gly, two Asp-Asn, two Asp-Asp, one Asp-Thr), among which the Asp-Gly sequences are particularly prone to aspartimide formation. Therefore, in a second attempt to synthesize MUB 70 , a systematic protection of each glycine amide moiety occurring before an Asp derivative was achieved by coupling Fmoc-Asp(OtBu)-(Dmb)Gly-OH dipeptides (29), namely in positions 29, 50, and 63, in reference to the C terminus ( Fig. 2A, Strategy 2).…”

Section: Identification Of Mubad or Mub 70 In L Reuteri Af120104mentioning

confidence: 99%

Design of a Specific Colonic Mucus Marker Using a Human Commensal Bacterium Cell Surface Domain

Coïc

Baleux

Poyraz

et al. 2012

Journal of Biological Chemistry

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Background: Imaging colonic mucus on living cells, tissues, and organs is required for live microscopy. Results: We have identified, synthesized, and validated a new human colonic mucus bacterial marker (MUB 70 ). Conclusion: This non-toxic marker is used to image the secreted colonic mucus. Significance: Beyond imaging applications, Cy5-MUB 70 might be used for diagnostic and prognosis applications on colonic mucinous carcinoma.

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Section: Identification Of Mubad or Mub 70 In L Reuteri Af120104mentioning

confidence: 99%

Design of a Specific Colonic Mucus Marker Using a Human Commensal Bacterium Cell Surface Domain

Coïc

Baleux

Poyraz

et al. 2012

Journal of Biological Chemistry

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“…The only problem of DBU usage is its ability to catalyze aspartimide formation from Asp [36]. However, certain side-chain carboxyl protection groups greatly reduce [43–46], and Asp-X peptide bond modifications exclude this side reaction [25, 33, 46], hence permitting the use of more efficient Fmoc removal catalyst in a greater set of difficult synthesis cases. …”

Section: Discussionmentioning

confidence: 99%

“…Hindered amino acid attachment to the growing peptide chain is typical for such peptides resulting in low yields of target products and a lot of byproducts represented by truncated peptides or peptides with gaps. These impurities are often difficult to separate from target products [23–25]. The problems of the “difficult” peptide synthesis are usually solved by (a) adding chaotropic salts or solvents [26, 27], (b) elevation of reaction mixture temperature via conventional heating or microwave irradiation [28–30], (c) use of more efficient catalysts of 9-fluorenyl(methoxycarbonyl) (Fmoc) N-terminal amino-protecting group removal and amino acid acylation [31, 32], and (d) prevention of the aggregation via introducing amido bond modifying groups [25, 33], isoacyl depsipeptide structures [34], and pseudoproline residues [35].…”

Section: Introductionmentioning

confidence: 99%

Development of the Schedule for Multiple Parallel “Difficult” Peptide Synthesis on Pins

Колесанова

Sanzhakov

Kharybin

2013

International Journal of Peptides

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Unified schedule for multiple parallel solid-phase synthesis of so-called “difficult” peptides on polypropylene pins was developed. Increase in the efficiency of 9-fluorenyl(methoxycarbonyl) N-terminal amino-protecting group removal was shown to have a greater influence on the accuracy of the “difficult” peptide synthesis than the use of more efficient amino acid coupling reagents such as aminium salts. Hence the unified schedule for multiple parallel solid-phase synthesis of “difficult” peptides included the procedure for N-terminal amino group deprotection modified by applying a more efficient reagent for the deprotection and the standard procedure of amino acid coupling by carbodiimide method with an additional coupling using aminium salts, if necessary. Amino acid coupling with the help of carbodiimide allows to follow the completeness of the coupling via the bromophenol blue indication, thus providing the accuracy of the synthesis and preventing an overexpenditure of expensive reagents. About 100 biotinylated hepatitis C virus envelope protein fragments, most of which represented “difficult” peptides, were successfully obtained by synthesis on pins with the help of the developed unified schedule.

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“…The main problem of this approach is the difficulty in the coupling of the residue following the Hmb auxiliary. In this sense, efforts have been directed to synthesizing less sterically hindered auxiliaries, such as the 2,4-dimethoybenzyl (Dmb)Gly [136] and the dicyclopropylmethyl (Dmcp) groups [137].…”

Section: Peg (3) Resinsmentioning

confidence: 99%

Methods for the Peptide Synthesis and Analysis

Tulla‐Puche

El‐Faham

Galanis

et al. 2015

Peptide Chemistry and Drug Design

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Application of Dmb-Dipeptides in the Fmoc SPPS of Difficult and Aspartimide-Prone Sequences

Cited by 57 publications

References 20 publications

Design of a Specific Colonic Mucus Marker Using a Human Commensal Bacterium Cell Surface Domain

Design of a Specific Colonic Mucus Marker Using a Human Commensal Bacterium Cell Surface Domain

Development of the Schedule for Multiple Parallel “Difficult” Peptide Synthesis on Pins

Methods for the Peptide Synthesis and Analysis

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