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Volumn 49, Issue 39, 2010, Pages 7049-7053

Traceless ligation of cysteine peptides using selective deselenization

Author keywords

Deselenization; Desulfurization; Native chemical ligation; Peptides; Protein modification

Indexed keywords

CYSTEINE RESIDUES; DESELENIZATION; NATIVE CHEMICAL LIGATION; PROTECTING GROUP; PROTEIN MODIFICATION; RADICAL INITIATORS; SELENOCYSTEINE; TRIS(2-CARBOXYETHYL) PHOSPHINE;

EID: 77956909658     PISSN: 14337851     EISSN: 15213773     Source Type: Journal    
DOI: 10.1002/anie.201001900     Document Type: Article
Times cited : (168)

References (70)
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    • The extension of desulfurization to other amino acids through β or υ thiol substitution was originally proposed in Ref. and has been shown for Abu, [7] Phe, and Val
    • The extension of desulfurization to other amino acids through β or υ thiol substitution was originally proposed in Ref. and has been shown for Abu, [7] Phe, and Val
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    • Reduced Sec peptides elute poorly from HPLC columns. The solvent free desulfurization of thiols by trialkylphosphites (and later phosphines) is inhibited by the presence of thiophenol
    • Reduced Sec peptides elute poorly from HPLC columns. The solvent free desulfurization of thiols by trialkylphosphites (and later phosphines) is inhibited by the presence of thiophenol
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    • Deselenization of Sec during native chemical ligation has been observed, Ref [15a]
    • Deselenization of Sec during native chemical ligation has been observed, Ref [15a].
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    • A minor side product of Sec to Ser conversion was observed, consistent with the Cys to Ser conversion observed in the free- radical-based desulfurization of Cys-Crotogossamide (Ref. [11]; Figure 54, page S36 in the Supporting Information). This side product is not observed under our optimized conditions with less TCEP.
    • A minor side product of Sec to Ser conversion was observed, consistent with the Cys to Ser conversion observed in the free- radical-based desulfurization of Cys-Crotogossamide (Ref. [11]; Figure 54, page S36 in the Supporting Information). This side product is not observed under our optimized conditions with less TCEP.
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    • The desulfurization of cysteines residues in proteins at elevated temperatures (up to 60 °C) with TCEP was observed by mass spectrometry, and is consistent with a thiyl radical-based mechanism
    • The desulfurization of cysteines residues in proteins at elevated temperatures (up to 60 °C) with TCEP was observed by mass spectrometry, and is consistent with a thiyl radical-based mechanism.
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    • The desulfurization of cysteines residues in proteins at elevated temperatures (up to 60 °C) with TCEP was observed by mass spectrometry, and is consistent with a thiyl radical-based mechanism. Z. Wang, T. Rejtar, Z. S. Zhou, B. L. Karger, Rapid Commun. Mass Spectrom. 2010, 24, 267-275.
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    • Wang, Z.1    Rejtar, T.2    Zhou, Z.S.3    Karger, B.L.4
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    • The desulfurized minor-product is likely to result from transfer of the selanyl radical to the Cys thiol, and subsequent desulfurization with TCEP as suggested by Danishefsky et al.[11]
    • The desulfurized minor-product is likely to result from transfer of the selanyl radical to the Cys thiol, and subsequent desulfurization with TCEP as suggested by Danishefsky et al.[11]
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    • The mechanism is thought to occur through attack of a selanyl radical with the phosphine TCEP to yield a phosphoranyl radical with an expanded valence shell. The homolytic cleavage of the C-Se bond forms an alkyl radical at the β-carbon, which abstracts hydrogen to form alanine. The driving force of the process is the formation of the strong Se=P bond.[27]
    • The mechanism is thought to occur through attack of a selanyl radical with the phosphine TCEP to yield a phosphoranyl radical with an expanded valence shell. The homolytic cleavage of the C-Se bond forms an alkyl radical at the β-carbon, which abstracts hydrogen to form alanine. The driving force of the process is the formation of the strong Se=P bond.[27]
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    • Recent attempts to reduce a seleno-α-conotoxin in the presence of excess reducing agents TCEP led to significant deselenization.
    • Recent attempts to reduce a seleno-α-conotoxin in the presence of excess reducing agents TCEP led to significant deselenization.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.