3017-32-1Relevant articles and documents
Investigating a Boronate-Affinity-Guided Acylation Reaction for Labelling Native Antibodies
Adak, Avijit K.,Huang, Kuan-Ting,Liao, Chien-Yu,Lee, Yuan-Jung,Kuo, Wen-Hua,Huo, Yi-Ren,Li, Pei-Jhen,Chen, Yi-Ju,Chen, Bo-Shiun,Chen, Yu-Ju,Chu Hwang, Kuo,Wayne Chang, Wun-Shang,Lin, Chun-Cheng
supporting information, (2022/02/22)
The excellent molecular recognition capabilities of monoclonal antibodies (mAbs) have opened up exciting opportunities for biotherapeutic discovery. Taking advantage of the full potential of this tool necessitates affinity ligands capable of conjugating directly with small molecules to a defined degree of biorthogonality, especially when modifying natural Abs. Herein, a bioorthogonal boronate-affinity-based Ab ligand featuring a 4-(dimethylamino)pyridine and an S-aryl thioester to label full-length Abs is reported. The photoactivatable linker in the acyl donor facilitated purification of azide-labelled Ab (N3-Ab) was quantitatively cleaved upon brief exposure to UV light while retaining the original Ab activity. Click reactions enabled the precise addition of biotin, a fluorophore, and a pharmacological agent to the purified N3-Abs. The resulting immunoconjugate showed selectivity against targeted cells. Bioorthogonal traceless design and reagentless purification allow this strategy to be a powerful tool to engineer native antibodies amenable to therapeutic intervention.
KETONE INHIBITORS OF LYSINE GINGIPAIN
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Paragraph 0269, (2018/04/12)
The present invention provides compounds according to Formula (I) as described herein, and their use for inhibiting the lysine gingipain protease (Kgp) from the bacterium Porphyromonas gingivalis. Also described are gingipain activity probe compounds and methods for assaying gingipain activity are also described, as well as methods for the treatment of disorders associated with P. gingivalis infection, including brain disorders such as Alzheimer's disease.
Simple and efficient Fmoc removal in ionic liquid
Di Gioia,Costanzo,De Nino,Maiuolo,Nardi,Olivito,Procopio
, p. 36482 - 36491 (2017/08/02)
A mild method for an efficient removal of the fluorenylmethoxycarbonyl (Fmoc) group in ionic liquid was developed. The combination of a weak base such as triethylamine and [Bmim][BF4] makes the entire system more efficient for the cleavage at room temperature of various amines and amino acid methyl esters in short reaction times. The procedure works well even in the case of N-Fmoc amino acids bearing acid-sensitive protecting groups and of N-alkylated amino acid methyl esters. The solvent-free condition provides a complementary method for Fmoc deprotection in solution phase peptide synthesis and modern organic synthesis.