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Polypeptides: Comparison
Please note this is a comparison between Version 3 by Jack Zhong and Version 2 by Catherine Yang.

Polypeptides are polymers of amino acids joined by amide bonds between the carboxyl group of one residue and the amino group of the next [1]. The backbone repeats over three atoms per residue, and the dihedral angles of that backbone decide whether the chain adopts an alpha-helix, a beta-sheet or a random coil [1]. Sequence, and not composition alone, fixes the conformation, so two polymers with identical amino acid content can fold differently [2]. Synthesis proceeds either by stepwise coupling of protected amino acids or by ring-opening polymerisation of N-carboxyanhydrides, and the routes differ in the control they give over sequence and dispersity [3]. The amide bond is cleaved by proteases, which makes the backbone degradable under physiological conditions [2].

  • amino acid sequence
  • alpha-helix
  • n-carboxyanhydride
  • amide backbone
  • proteolytic cleavage

References

  1. Lv, H.; Zhang, X.; Zhao, Y.; Cheng, J. Advances in polypeptide synthesis. Science China Chemistry 2025, 68, 5527-5540. [CrossRef]
  2. Chen, Z.; Zhou, Z.; Zeng, M.; Bao, Y.; Deng, Y.; Li, S.; Luo, X.; He, N. Novel Polypeptide Automated Synthesis Devices: A Review. Journal of Biomedical Nanotechnology 2024, 20, 1062-1075. [CrossRef]
  3. Deming, T.J. Polypeptide and Polypeptide Hybrid Copolymer Synthesis via NCA Polymerization. ChemInform 2007, 38, chin.200705228. [CrossRef]
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