87176-71-4Relevant academic research and scientific papers
The urea-dipeptides show stronger H-bonding propensity to nucleate β-sheetlike assembly than natural sequence
Ke, Damei,Zhan, Chuanlang,Li, Xiao,Li, Alexander D.Q.,Yao, Jiannian
experimental part, p. 8269 - 8276 (2009/12/26)
In this article, we report the distinct solution behavior of a set of urea-dipeptides to that of natural sequence. The urea-dipeptides adopt β-folding conformations and form into β-sheetlike assembly in chloroform. Most surprisedly, the urea-dipeptides tend to form interpeptide H-bonding interactions even at a concentration of as low as 0.1 mM, while the natural sequence shows H-bonding propensity at a concentration of about 7 mM, indicating that the urea-dipeptides show much stronger H-bonding propensity to nucleate formation of β-sheetlike assembly than the natural sequence. CD spectra reveal that the investigated urea-dipeptides have two negative CD bands, respectively, around 217 nm and 224 nm, supporting the β-folding conformations and in turn formation of β-sheetlike assembly. The β-sheetlike assembly is also confirmed by the XRD reflections, which give two typical d-spacings of 12.7 and 4.8 A?, respectively, corresponding to stacking periodicity of the β-sheets and the spacing between peptide backbones running orthogonal to the β-sheet axis.
DI- AND TRIPEPTIDE N-ALKYL- AND N-ARALKYL AMIDES AS CHYMOTRYPSIN INHIBITORS
Kasafirek, Evzen,Sutiakova, Irena,Bartik, Michal,Sturc, Antonin
, p. 2877 - 2883 (2007/10/02)
Two competitive inhibitors of chymotrypsin, Glt-Ala-Ala-Leu-EtPh and Glt-Ala-Ala-Pro-NH-EtPh, were synthesized and their inhibition constants Ki were determined.The Ki-determination was carried also with a set of peptides of type X-(
