<?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%">Kamble, Sandip Sushila Mohan</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-triazolobenzodiazepine hybrids: a catalyst-free on-resin strategy to build complex therapeutic motifs into peptides</style></title><secondary-title><style face="normal" font="default" size="100%">Chemistry-A European Journal</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">hybrid peptides</style></keyword><keyword><style  face="normal" font="default" size="100%">peptide chemistry</style></keyword><keyword><style  face="normal" font="default" size="100%">peptide modification</style></keyword><keyword><style  face="normal" font="default" size="100%">spps compatibility</style></keyword><keyword><style  face="normal" font="default" size="100%">triazolobenzodiazepines</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2025</style></year><pub-dates><date><style  face="normal" font="default" size="100%">JUN</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">31</style></volume><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;
	The merger of peptide and heterocyclic chemistry presents significant opportunities for enhancing the structural and functional diversity of therapeutic agents. In this study, we introduce a streamlined on-resin method to modify peptides at the N-terminus amines and the side chain amines of Lys/Orn amino acids by incorporating the biologically active triazolobenzodiazepine scaffold. In the presented solid-phase peptide synthesis (SPPS), the triazolobenzodiazepine core is formed on-resin through a combination of N-alkylation, amide bond formation, and an alkyne-azide 1,3-dipolar cycloaddition, of which the latter two happen as a single-step one-pot reaction- proceeding under mild conditions without metal catalysts. This protocol tolerates a wide variety of amino acids and functional groups, providing a versatile method for synthesizing peptide-triazolobenzodiazepine hybrids. Using orthogonal protection group strategies, we further demonstrate the method's adaptability for two site modifications in peptides involving both the N-terminus and Lys side chain amines. These modifications enhance the scope of ``peptide medicinal chemistry'' by creating multifunctional peptides with potential therapeutic applications. The method's compatibility with SPPS, room temperature conditions, and elimination of metal catalysis make it an efficient and powerful tool for peptide modification.&lt;/p&gt;
</style></abstract><issue><style face="normal" font="default" size="100%">34</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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	3.7&lt;/p&gt;
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