82252-39-9

Usage

Uses

Used in Pharmaceutical and Biotechnology Industries:
BOC-LEU-(R)-VAL-OH is used as a key component in peptide synthesis for its ability to enhance the stability and solubility of peptides. This is vital for the development of effective drug formulations and therapeutic agents.
Used in Drug Development and Research:
In the realm of drug development, BOC-LEU-(R)-VAL-OH serves as a crucial building block for the synthesis of bioactive peptides, which can be used to target specific biological pathways and diseases.
Used in Controlling Stereochemistry of Peptide Synthesis:
BOC-LEU-(R)-VAL-OH is also utilized to control the stereochemistry during peptide synthesis, ensuring that the final product has the correct spatial arrangement of atoms, which is essential for biological activity and selectivity.
Overall, BOC-LEU-(R)-VAL-OH is an important chemical in the field of biochemistry and medicine, playing a pivotal role in the synthesis of peptides and proteins with potential therapeutic applications.

Upstream product

• 82252-38-8 N^α-Boc-LeuΨVal-OBzl 
• 13139-15-6 N-tert-butoxycarbonyl-L-leucine 
• 21760-98-5 L-valine benzyl ester 

Relevant academic research and scientific papers

Design, Structure-Activity, and Molecular Modeling Studies of Potent Renin Inhibitory Peptides Having N-Terminal Nin-For-Trp (Ftr): Angiotensinogen Congeners Modified by P1-P1' Phe-Phe, Sta, LeuΨVal or LeuΨVal Substitutions

A structure-conformation-activity investigation of several angiotensinogen (ANG) based inhibitors of human renin modified by either Phe-Phe, Sta, LeuΨVal, or LeuΨVal at the P1-P1' cleavage site and P5 Trp(Nin-For) (Ftr) was performed.Specifically, Ac-Ftr-Pro-Phe-His-Phe-Phe-Val-Ftr-NH2 (1) provided a potent (KI = 2.7 x 10-8 M) P1-P1' Phe-Phe substituted renin inhibitor to initiate these studies.Substitution of the P1-P1' Phe-Phe in compound 1 by Sta effected a 1000-fold increase in biological potency for the resultant octapeptide Ac-Ftr-Pro-Phe-His-Sta-Val-Ftr-NH2 (10; KI = 6.7 x 10-11 M).Kinetic analysis of compound 10 showed it to be a competitive inhibitor of human renin catalyzed proteolysis of human ANG.Chemical modifications of the compounds 1 and 10 were evaluated on the basis of comparative human plasma renin inhibitory activities (IC 50 values) in vitro.Carboxy-terminal truncation studies on compound 10 showed that the P2' Val and P3' Ftr residues could both be eliminated without significant loss (ca. 10-fold) in renin inhibitory activity as exemplified by the pentapeptide Ac-Ftr-Pro-Phe-His-Sta-NH2 (12; IC 50 = 3.8 x 10-9 M).In addition, the corresponding P1-P1' LeuψVal and LeuψVal derivatives of compound 12 were potent renin inhibitors: Ac-Ftr-Pro-Phe-His-LeuψVal-NH2 (13; IC 50 = 3.1 x 10-10 M) and Ac-Ftr-Pro-Phe-His-LeuψVal-NH2 (14; IC 50 = 2.1 x 10-8 M).The structure-conformation-activity properties of the N-terminal Ftr substitution of these human renin inhibitors was examined by (1) comparative analysis of several analogues of 1 and Ac-Ftr-Pro-Phe-His-Sta-Ile-NH2 (17; IC 50 = 1.0 x 10-10 M) having P5 site modifications by Trp, His, D-Ftr and D-His, (2) deletion of the N-terminal Ftr residue from compound 12 and 17, to provide Ac-Pro-Phe-His-Sta-Ile-NH2 (16; IC 50 = 3.1 x 10-8 M) and Ac-Pro-Phe-His-Sta-NH2 (15; IC 50 = 5.6 x 10-6 M), and (3) computer modeling and dynamic studies of compounds 1 and 17 bound to CKH-RENIN, a simulated human renin model, which were focused on identifying potentional intermolecular interactions of their common P5-P2 sequence, Ac-Ftr-Pro-Phe-His, at the enzyme active site.Finally, the human renin specificity of selected congeners of compound 10 were determined by comparison to porcine kidney renin in vitro.