124322-07-2Relevant academic research and scientific papers
Conformationally Constrained Renin Inhibitory Peptides: Cyclic (3-1)-1-(Carboxymethyl)-L-prolyl-L-phenylalanyl-L-histidinamide as a Conformational Restriction at the P2-P4 Tripeptide Portion of the Angiotensinogen Template
Thaisrivongs, Suvit,Blinn, James R.,Pals, Donald T.,Turner, Steve R.
, p. 1276 - 1282 (2007/10/02)
Interest in conformationally constrained peptides as potential inhibitors of renin led us to examine an N-terminal cycle of linear renin inhibitory peptides.A cyclic structure was prepared by joining the N-terminal proline at the P4 site to the imidazole
Renin Inhibitory Peptides. A β-Aspartyl Residue as a Replacement for the Histidyl Residue at the P-2 Site
Thaisrivongs, Suvit,Mao, Boryeu,Pals, Donald T.,Turner, Steve R.,Kroll, Lisa T.
, p. 1337 - 1343 (2007/10/02)
In an effort to decrease the size and to increase the hydrophilicity of the previously prepared renin inhibitory peptides, it was postulated that one might be able to take advantage of the polar Thr-84 on the flap region of the enzyme renin by potential h
