174799-89-4Relevant articles and documents
Tuning of protease resistance in oligopeptides through: N -alkylation
Kaminker, Revital,Anastasaki, Athina,Gutekunst, Will R.,Luo, Yingdong,Lee, Sang-Ho,Hawker, Craig J.
supporting information, p. 9631 - 9634 (2018/09/10)
N-Methylation of amino acids is an effective way to create protease resistance in both natural and synthetic peptides. However, alkyl substituents other than N-methyl have not been extensively studied. Here, we prepare and examine a series of N-substituted peptides in which the size and length of the alkyl group is modulated. These design insights provide a unique and modular handle for tuning proteolysis in oligopeptides.
Gadolinium-binding cyclic hexapeptoids: Synthesis and relaxometric properties
De Cola, Chiara,Fiorillo, Gaetano,Meli, Alessandra,Aime, Silvio,Gianolio, Eliana,Izzo, Irene,De Riccardis, Francesco
, p. 424 - 431 (2014/01/06)
Two new cyclic hexapeptoids incorporating N-carboxyethylglycine and N-methoxyethylglycine residues are able to efficiently bind Gd3+. Their thermodynamic stabilities and relaxivities have been assessed by 1H-relaxometric investigatio
