37827-06-8

Usage

Uses

Used in Pharmaceutical Industry:
SAR-ARG-VAL-TYR-ILE-HIS-PRO-ILE is used as a therapeutic agent for its potential role in treating specific health conditions. The peptide sequence may contribute to the development of new medications due to its involvement in muscle growth, repair, and immune function, offering a targeted approach to various diseases and disorders.
Used in Sports Nutrition:
In the sports nutrition industry, SAR-ARG-VAL-TYR-ILE-HIS-PRO-ILE is used as a supplement to enhance muscle growth and repair. Its role in physiological processes related to muscle development makes it a valuable component in products designed to support athletes and fitness enthusiasts in achieving their performance goals.
Used in Hormone Production Regulation:
SAR-ARG-VAL-TYR-ILE-HIS-PRO-ILE is utilized as a regulatory component in hormone production. Given its influence on physiological processes, this peptide can be employed in formulations aimed at balancing or enhancing hormone levels, which can be particularly beneficial for conditions related to hormonal imbalances.
Used in Immune Function Enhancement:
In the field of immunology and related health applications, SAR-ARG-VAL-TYR-ILE-HIS-PRO-ILE is used to boost immune function. Its role in the immune system suggests potential uses in immune-strengthening therapies or products designed to improve resistance against infections and diseases.

Upstream product

• 13734-41-3 t-Boc-L-valine 
• 13734-36-6 N-(tert-butoxycarbonyl)sarcosine 
• 13726-76-6 t-butyloxycarbonyl-L-arginine 
• 3978-80-1 Boc-Tyr-OH 
• 15761-39-4 1-(tert-butoxycarbonyl)-L-proline 
• 13139-16-7 N-(tert-butyloxycarbonyl)-L-isoleucine 
• 17791-52-5 (S)-2-tert-Butoxycarbonylamino-3-(3H-imidazol-4-yl)-propionic acid 
• 35899-43-5 Boc-His(Tos)-OH 

Relevant academic research and scientific papers

An Investigation of Angiotensin II Agonist and Antagonist Analogues with 5,5-Dimethylthiazolidine-4-carboxylic Acid and Other Constrained Amino Acids

The probe the receptor-bound conformational requirements of angiotensin II (ANG II) octapeptide and antagonists, the synthesis and biological activities of 1>ANG II agonist and 1,X8>ANG II antagonist analogues (X8 = Ile, D-Phe, or Aib) bearing conformational constraints in positions 3, 5, and 7 were investigated and compared with previous literature efforts.The conformational constraints that were examined include Pro, Dtc (5,5-dimethylthiazolidine-4-carboxylic acid), Aib, Cle, (NMe)Ala, (NMe)Ile, and the lactam modification, L,L-lactam-Phe, previouslydescribed by Freidinger et al. (J.Org.Chem. 1982, 47, 104-109).Both 1,(NMe)Ala3, and Pro3>ANG II retained agonist activity, while only 1,(NMe)Ala3,Ile8>ANG II retained antagonistic activity. 1,Dtc5>ANG II displayed superior agonist activity, while both 1,Dtc5 and Cle5,Ile8>ANG II displayed superior antagonist activity. In contrast to position 5, Dtc7 substitution for Pro7 of either 1>ANG II or 1,Ile8>ANGII gave analogues with reduced activities.These results are consistent with the hypothesis that confirmations of 1>ANG II and 1,Ile8>ang II containing a C7 conformation in position 7 are preferred for both ANG II agonist and antagonist activity.Incorporation of the L,L-lactam-Phe modification into 1>ANG II gives a pure ANG antagonist (pA2 8.3), comparable to saralasin pA2 8.6).In position 3, 5, and 7 the conformational requirements for the ANG IIagonist 1>ANG II and the ANG II antagonist 1,Ile8>ANG II may be different.Individual substitution of (NMe)Ala3, Dtc5, D-Phe8 and Aib8 1,Aib8>ANG II: Kosla et al.J.Med.Chem. 1972, 20, 1051-1055> into 1,Ile8>ANG II gives that retain antagonistic activity.Multiple substitutions of these types of residues into 1,Ile8>ANG II gives analogue 45 1,(NMe)Ala3,Dtc5,Aib8>ANG II, 46 1(NMe)Ala3,D-Phe8>AII, and 47 1,Dtc5,D-Phe8>AII, which display considerably reduced antagonist activity.In ANG II antagonist the construction of highly constrained analogues may not be possible by the additive substitution of "preferred" constrained amino acids into a single analogue.

Potent Angiotensin II Antagonists with Non-β-branched Aminoacids in Position 5

Amino acids with lipophilic side chains that contain more than one functional group on the β-carbon, i.e. a β-branched hydrocarbon moiety, are required in position 5 of angiotensin II (AII) analogue with potent agonist activity.This requirement for agonis

Structure-Activity Relationships for the Competitive Angiotensin Antagonist 1,O-methyltyrosine4>angiotensin II (Sarmesin)

Analogues of the competitive angiotensin antagonist 1,Tyr(Me)4>ANG II (sarmesin) in which the sarcosine-1, O-methyltyrosine-4, and phenylalanine-8 residues were modified have been synthesized by the solid-phase method.The agonist and antagonist potencies of the 23 peptides synthesized were determined in the rat isolated uterus assay.At position 1, replacement of Sar with Asp, Ala, or Pro gave inactive analogues, and deletion of the N-terminal amino acid produced inactive heptapeptides for all analogues investigated.At position 4, substitution of Tyr with Tyr(Et), D-Tyr, D-Phe, Ile, Thr, or Hyp resulted in inactive analogues, whereas substitution of Phe gave a potent competitive antagonist (pA2 = 7.9), which retained significant agonist activity (22percent).For position 8, 1,Tyr(Me)4,Ile8>ANG II and 1,Phe4,Ile8>ANG II were weaker antagonists (pA2 = 6.6 and 6.7, respectively) than 1,Ile8>ANG II (pA2 apparent = 8,1) and moreover, were reversible competitive antagonists.These findings demonstrate that the structural requirements for receptor blockade by sarmesin are remarkably stringent-modifications at positions 1, 4, and 8 markedly reduce the antagonist activity of this peptide.