Site-specific labelling of native peptides and proteins: chemical and enzymatic strategies

• Antonio Angelastro,
• Jonathan Bargh,
• Subhajit Guria,
• Victor Laserna and
• Louis Luk

Beilstein J. Org. Chem. 2026, 22, 857–881, doi:10.3762/bjoc.22.67

• highlight opportunities for innovation in next-generation native-sequence protein modification technologies. Keywords: affinity-guided chemistry; disulfide-rebridging; enzyme catalysis; glycan modifications; native-sequence; protein labelling; small-molecule modifications; terminal; Introduction Protein

• influence labelling efficiency; this is often the case for N-terminal and glycan modifications where composition of the protein may vary with the recombinant host. Protein precipitation and unintended side reactions, which are often underreported, can further complicate the anticipated outcome. The

Semiautomated glycoproteomics data analysis workflow for maximized glycopeptide identification and reliable quantification

• Steffen Lippold,
• Arnoud H. de Ru,
• Jan Nouta,
• Peter A. van Veelen,
• Magnus Palmblad,
• Manfred Wuhrer and
• Noortje de Haan

Beilstein J. Org. Chem. 2020, 16, 3038–3051, doi:10.3762/bjoc.16.253

• identify all glycopeptides in a cluster. The clusters are also presented in interactive graphs, which assist in the identification of false-positive connections (unlikely mass/RT shifts) and unexpected glycopeptide clusters (e.g., missed cleaved products and peptide or glycan modifications). This

GlypNirO: An automated workflow for quantitative N- and O-linked glycoproteomic data analysis

• Toan K. Phung,
• Cassandra L. Pegg and
• Benjamin L. Schulz

Beilstein J. Org. Chem. 2020, 16, 2127–2135, doi:10.3762/bjoc.16.180

• peptide. For N-linked searches (N-X-S/T) a database of 164 N-glycans was used (Supporting Information File 1, Table S41) and for the O-linked searches (at any S/T) a database of 49 O-glycans (Supporting Information File 1, Table S42) was used. All glycan modifications were set as “Rare 1” allowing each

Synthesis of Streptococcus pneumoniae serotype 9V oligosaccharide antigens

• Sharavathi G. Parameswarappa,
• Claney L. Pereira and
• Peter H. Seeberger

Beilstein J. Org. Chem. 2020, 16, 1693–1699, doi:10.3762/bjoc.16.140

• vaccines. The serotype 9V is part of the currently marketed conjugate vaccine and contains an acetate modification. To better understand the importance of glycan modifications in general and acetylation in particular, defined oligosaccharide antigens are needed for serological and immunological studies

Molecular architecture with carbohydrate functionalized β-peptides adopting 3₁₄-helical conformation

• Nitin J. Pawar,
• Navdeep S. Sidhu,
• George M. Sheldrick,
• Dilip D. Dhavale and
• Ulf Diederichsen

Beilstein J. Org. Chem. 2014, 10, 948–955, doi:10.3762/bjoc.10.93

• carbohydrate derived α,β-unsaturated ester [47][48][49][50]. In the present article, a new class of C-linked β-glycopeptide scaffolds 1–8 (Figure 2) were synthesized and investigated with respect to secondary structures, along with the influence of glycan modifications on peptide conformation [24][25], and the