ArticleProceedings of the National Academy of Sciences of the United States of America2000
Chemical synthesis and spontaneous folding of a multidomain protein: anticoagulant microprotein S.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 37 citations in OpenAlex.
- Advances in the chemical synthesis of human proteoforms.Science China. Life sciences · 2025Review
- AaTs-1: A Tetrapeptide fromMolecules (Basel, Switzerland) · 2021Article
- Native chemical ligation: a boon to peptide chemistry.Molecules (Basel, Switzerland) · 2014Review
- IL-32 promotes angiogenesis.Journal of immunology (Baltimore, Md. : 1950) · 2014Article
- Protein S protects neurons from excitotoxic injury by activating the TAM receptor Tyro3-phosphatidylinositol 3-kinase-Akt pathway through its sex hormone-binding globulin-like region.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2010Article
- Expression, purification and ligand binding properties of the recombinant translation initiation factor (PeIF5B) from Pisum sativum.Molecular and cellular biochemistry · 2010Article
- Characterization of LEF4 ligand binding property and its role as part of baculoviral transcription machinery.Molecular and cellular biochemistry · 2010Article
- Synthesis of an iberiotoxin derivative by chemical ligation: a method for improved yields of cysteine-rich scorpion toxin peptides.Peptides · 2009Article
- The thrombin-sensitive region of protein S mediates phospholipid-dependent interaction with factor Xa.The Journal of biological chemistry · 2008Article
- Chemical synthesis of proteins.Annual review of biophysics and biomolecular structure · 2005Review
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Because of recent high-yield native ligation techniques, chemical synthesis of larger multidomain bioactive proteins is rapidly coming within reach. Here we describe the total chemical synthesis of a designed "microprotein S," comprising the gamma-carboxyglutamic acid-rich module, the thrombin-sensitive module, and the first epidermal growth factor-like module of human plasma protein S (residues 1-116). Synthetic microprotein S expressed anticoagulant cofactor activity for activated protein C in the down-regulation of blood coagulation, and the anticoagulant activity of microprotein S was not neutralized by C4b-binding protein, a natural inhibitor of native protein S in plasma. The correct folding of this complex multidomain protein was enhanced compared with individual modules because the gamma-carboxyglutamic acid-rich module and the thrombin-sensitive module markedly facilitated correct folding of the first epidermal growth factor-like module compared with folding of the first epidermal growth factor-like module alone. These results demonstrate that total chemical synthesis of proteins offers an effective way to generate multidomain biologically active proteins.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.