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Cited by 197Chemical Synthesis and AnalysisEnzyme Catalysis and ImmobilizationAdvanced Polymer Synthesis and Characterization

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Formation of oligopeptides in high yield under simple programmable conditions

Open access
Rodriguez-Garcia, Marc, Surman, Andrew J., Cooper, Geoffrey J.T., Suárez-Marina, Irene, Hosni, Zied, Lee, Michael P., Cronin, Leroy·2015·Nature Communications
DOI 10.1038/ncomms9385PMC PMC4633627
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Abstract

Many high-yielding reactions for forming peptide bonds have been developed but these are complex, requiring activated amino-acid precursors and heterogeneous supports. Herein we demonstrate the programmable one-pot dehydration–hydration condensation of amino acids forming oligopeptide chains in around 50% yield. A digital recursive reactor system was developed to investigate this process, performing these reactions with control over parameters such as temperature, number of cycles, cycle duration, initial monomer concentration and initial pH. Glycine oligopeptides up to 20 amino acids long were formed with very high monomer-to-oligomer conversion, and the majority of these products comprised three amino acid residues or more. Having established the formation of glycine homo-oligopeptides, we then demonstrated the co-condensation of glycine with eight other amino acids (Ala, Asp, Glu, His, Lys, Pro, Thr and Val), incorporating a range of side-chain functionality.

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  • Other groups have demonstrated polypeptide formation through wet-dry cycling.

    “Other groups have demonstrated polypeptide formation through wet-dry cycling (Forsythe et al., 2015; Rodriguez-Garcia et al., 2015).”

    From The Hot Spring Hypothesis for an Origin of Life (2020) · cites this paper as Rodriguez-Garcia et al., 2015

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Research works printed but not linked: 26

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Metadata

Authors
Rodriguez-Garcia, M., Surman, A. J., Cooper, G. J. T., Suárez-Marina, I., Hosni, Z., Lee, M. P., & Cronin, L.
Affiliations
University of Glasgow (GB)
Corresponding author
Cronin, Leroy
ORCID
Venue
Nature Communications
Publisher
Springer Science and Business Media LLC
Published
2015-10-07
Volume
6
Issue
1
Pages
8385-8385
ISSN
2041-1723 (ISSN-L)
DOI
10.1038/ncomms9385
PMC
PMC4633627
OpenAlex
W2229162150
Cited by
197
References
5
Citations by year
2026: 14 · 2025: 13 · 2024: 17 · 2023: 15 · 2022: 21 · 2021: 27 · 2020: 21 · 2019: 20 · 2018: 21 · 2017: 16 · 2016: 10 · 2015: 1
FWCI
6.78
Type
journal article
Language
en
Open access
Licence
Locations
  • Nature Communications (publishedVersion, cc-by)
  • Europe PMC (PubMed Central) (publishedVersion, cc-by)
  • PubMed Central (publishedVersion, cc-by)
  • PubMed (publishedVersion)
  • ENLIGHTEN (Jurnal Bimbingan dan Konseling Islam) (acceptedVersion)
  • RePEc: Research Papers in Economics (submittedVersion)
  • Research Portal (King's College London) (submittedVersion, other-oa)
Funders
Engineering and Physical Sciences Research Council (EP/I033459/1, EP/J015156, EP/H024107/1, EP/J015156/1)
Topics
  • Physical Sciences › Chemistry › Organic Chemistry › Chemical Synthesis and Analysis
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Enzyme Catalysis and Immobilization
  • Physical Sciences › Chemistry › Organic Chemistry › Advanced Polymer Synthesis and Characterization
Keywords
peptide bond formation, one-pot synthesis, peptide synthesis
MeSH terms
Amino Acids, Automation, Chromatography, High Pressure Liquid, Oligopeptides, Mass Spectrometry, Organic Chemistry Phenomena, Chromatography, Reverse-Phase, Chemistry Techniques, Synthetic

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