40958-31-4Relevant articles and documents
Programming Bioactive Architectures with Cyclic Peptide Amphiphiles
Kuan, Seah Ling,Wang, Tao,Raabe, Marco,Liu, Weina,Lamla, Markus,Weil, Tanja
, p. 1347 - 1353 (2015)
We present a versatile approach for the synthesis of cyclic peptide amphiphiles of the hormone somatostatin (SST) with tunable lipophilic tails to program bioactive nanoarchitectures. A novel bis-alkylation reagent is synthesized that facilitates the functionalization of SST with a thiol anchor. Different hydrophobic moieties are introduced inspired by a biomimetic palmitoylation approach which opens access to cyclic peptide amphiphiles that display rich self-organization and cell membrane interactions. Made to order: Cyclic peptide amphiphiles prepared by a bioinspired approach are employed to program various bioactive nanoarchitectures that display rich self-organization and cell membrane interactions.
Robust synthesis of C-terminal cysteine-containing peptide acids through a peptide hydrazide-based strategy
Zuo, Chao,Yan, Bing-Jia,Zhu, Han-Ying,Shi, Wei-Wei,Xi, Tong-Kuai,Shi, Jing,Fang, Ge-Min
supporting information, p. 5698 - 5702 (2019/06/18)
A new robust strategy was reported for the epimerization-free synthesis of C-terminal Cys-containing peptide acids through mercaptoethanol-mediated hydrolysis of peptide thioesters prepared in situ from peptide hydrazides. This simple-to-operate and highly efficient method avoids the use of derivatization reagents for resin modification, thus providing a practical avenue for the preparation of C-terminal Cys-containing peptide acids.
Aryloxymaleimides for cysteine modification, disulfide bridging and the dual functionalization of disulfide bonds
Marculescu, Cristina,Kossen, Hanno,Morgan, Rachel E.,Mayer, Patrick,Fletcher, Sally A.,Tolner, Berend,Chester, Kerry A.,Jones, Lyn H.,Baker, James R.
supporting information, p. 7139 - 7142 (2014/07/07)
Tuning the properties of maleimide reagents holds significant promise in expanding the toolbox of available methods for bioconjugation. Herein we describe aryloxymaleimides which represent 'next generation maleimides' of attenuated reactivity, and demonstrate their ability to enable new methods for protein modification at disulfide bonds.