ArticleACS central science2025
Chemical Synthesis and Chaperone Peptide Mediated Folding of Human Nerve Growth Factor by Expressed KAHA Ligation.
Article in ACS central science, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
3 citing papers in PubMed.
- Neuroimmune regulation of post-traumatic bone regeneration: focus on inflammatory switching and functional recovery.Frontiers in immunology · 2026Review
- Cyclic Hydroxylamines for Native Residue-Forming Peptide Ligations: Synthesis of Ubiquitin and Tirzepatide.Journal of the American Chemical Society · 2025Article
- Backbone Protecting Groups for Enhanced Peptide and Protein Synthesis.Angewandte Chemie (International ed. in English) · 2025Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Nerve growth factor (NGF) is a powerful neurotrophic protein for treating central nervous system diseases, but its therapeutic utility is limited by severe side effects, including hyperalgesia. These adverse effects arise from pleitropic receptor binding that can, in principle, be modulated by side chain mutations or modificationa task suited for chemical protein synthesis. Despite its small size (13 kDa), the chemical synthesis of NGF has been stymied by exceptional hydrophobicity and the requirement for a 104-residue N-terminal "chaperone peptide" for folding. This study presents a chemical synthesis of NGF using α-ketoacid-hydroxylamine (KAHA) ligations, featuring recombinant production of the chaperone peptide and its chemoselective conversion to a C-terminal α-ketoacid. A novel solubility tag, SOLACE, and ester-forming KAHA ligations enabled assembly of linear proNGF from three synthetic and one recombinant segment. Controlled folding and disulfide-bond formation mediated by the chaperone peptide followed by proteolytic cleavage yielded biologically active synthetic NGF as its noncovalent dimer. The synthetic NGF exhibited comparable activity to recombinant NGF in axon growth assays, establishing a platform for engineering NGF variants with tailored therapeutic properties. This approach provides a versatile framework for the semisynthesis of neurotrophins and related proteins that also require long chaperone peptides for proper folding.
Identifiers
What OpenQuestion holds
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.