<?xml version="1.0" encoding="UTF-8"?><xml><records><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Shinde, Dinesh R.</style></author><author><style face="normal" font="default" size="100%">Bodake, Supriya Mahadev</style></author><author><style face="normal" font="default" size="100%">Marelli, Udaya Kiran</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Peptide functionalization with dithioate and trithioate groups: A CS2-mediated solid-phase approach</style></title><secondary-title><style face="normal" font="default" size="100%">Organic Letters</style></secondary-title></titles><dates><year><style  face="normal" font="default" size="100%">2025</style></year><pub-dates><date><style  face="normal" font="default" size="100%">MAY </style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">27</style></volume><pages><style face="normal" font="default" size="100%">6271-6278</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;
	The dithiocarbamate group is an important class of compounds whose presence in small molecules and peptides leads to antimicrobial, anticancer, and enzyme inhibition properties. This study introduces an efficient and selective method for incorporating dithioate and trithioate moieties into amino acids and peptides using CS2 chemistry under mild conditions. Utilizing a N,N-diisopropylethylamine (DIPEA)-CS2-benzyl chloride system, we achieved modifications at the N-terminal amines and the side chains of Lys and Cys residues through solid-phase peptide synthesis (spps). The method exhibits excellent yields and broad compatibility with diverse amino acids, their protection groups, peptide chemistry reagents, and varied peptide sequences. Notably, the successful incorporation of trithioate groups into peptides via cysteines, reported here for the first time, expands the functional repertoire of peptide chemistry, offering new possibilities for peptide-based drug design and related applications.&lt;/p&gt;
</style></abstract><issue><style face="normal" font="default" size="100%">24</style></issue><work-type><style face="normal" font="default" size="100%">Article</style></work-type><custom3><style face="normal" font="default" size="100%">&lt;p&gt;
	Foreign&lt;/p&gt;
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	4.6&lt;/p&gt;
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