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Peptide ligations accelerated by N-terminal aspartate and glutamate residues.

Thomas, Gemma L. (author)
Hsieh, Yves S. Y. (author)
University of Sydney, Australia
Chun, Candy K. Y. (author)
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Cai, Zheng-Li (author)
Reimers, Jeffrey R. (author)
Payne, Richard J. (author)
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 (creator_code:org_t)
2011-08-10
2011
English.
In: Organic Letters. - : American Chemical Society (ACS). - 1523-7060 .- 1523-7052. ; 13:18, s. 4770-3
  • Journal article (peer-reviewed)
Abstract Subject headings
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  • A novel application of intramolecular base catalysis confers enhanced reaction rates for aminolysis ligations between peptide thioesters and peptides bearing N-terminal aspartate or glutamate residues. The broad scope of this process and its application in the total synthesis of the diabetes drug exenatide is demonstrated.

Subject headings

NATURVETENSKAP  -- Kemi -- Organisk kemi (hsv//swe)
NATURAL SCIENCES  -- Chemical Sciences -- Organic Chemistry (hsv//eng)

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art (subject category)

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