title: Chemical Synthesis of HMGA1a Proteins with Post-translational Modifications via Ser/Thr Ligation.
abstract: The first chemical synthesis of nuclear protein HMGA1a via Ser/Thr ligation is reported. Notably, Hmb (2-hydroxy-4-methoxybenzyl) exhibits crucial improvement of both the difficult coupling during solid phase peptide synthesis and the poor ligation encountered in protein synthesis. These efforts led to preparation of HMGA1a analogs with well-defined phosphorylation and methylation patterns (9 synthetic proteins in total), thus overcoming the heterogeneous and combinatory problems inherent to protein post-translational modifications (PTMs), and facilitating the study of the regulatory roles of such PTMs.
authors.affiliation: Department of Chemistry, State Key Lab of Synthetic Chemistry, The University of Hong Kong , Pokfulam, Hong Kong.
authors.forename: Tianlu
authors.initials: T
authors.lastname: Li
authors.affiliation: Department of Chemistry, State Key Lab of Synthetic Chemistry, The University of Hong Kong , Pokfulam, Hong Kong.
authors.forename: Heng
authors.initials: H
authors.lastname: Liu
authors.affiliation: Department of Chemistry, State Key Lab of Synthetic Chemistry, The University of Hong Kong , Pokfulam, Hong Kong.
authors.forename: Xuechen
authors.initials: X
authors.lastname: Li
mesh_terms: D000595:Amino Acid Sequence; D025741:HMGA1a Protein / Q000138:chemical synthesis* / Q000737:chemistry; D015394:Molecular Structure; D010446:Peptide Fragments / Q000138:chemical synthesis* / Q000737:chemistry; D010766:Phosphorylation; D011499:Protein Processing, Post-Translational; D012694:Serine / Q000737:chemistry*; D060327:Solid-Phase Synthesis Techniques / Q000379:methods*; D013912:Threonine / Q000737:chemistry*
chemical_list: D010446:Peptide Fragments; D025741:HMGA1a Protein; D013912:Threonine; D012694:Serine