Val-Arg

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Val-Arg
Category Others
Catalog number BBF-05162
CAS 37682-75-0
Molecular Weight 273.33
Molecular Formula C11H23N5O3

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Specification

Synonyms L-valyl-L-arginine; valylarginine; VR dipeptide; L-Val-L-Arg; Valine Arginine dipeptide
Sequence H-Val-Arg-OH
Storage Store at -20°C
IUPAC Name (2S)-2-[[(2S)-2-amino-3-methylbutanoyl]amino]-5-(diaminomethylideneamino)pentanoic acid
Canonical SMILES CC(C)C(C(=O)NC(CCCN=C(N)N)C(=O)O)N
InChI InChI=1S/C11H23N5O3/c1-6(2)8(12)9(17)16-7(10(18)19)4-3-5-15-11(13)14/h6-8H,3-5,12H2,1-2H3,(H,16,17)(H,18,19)(H4,13,14,15)/t7-,8-/m0/s1
InChI Key IBIDRSSEHFLGSD-YUMQZZPRSA-N

Properties

Density 1.36±0.1 g/cm3

Reference Reading

1. Biochemical property and in vivo efficacies of novel Val/Arg-rich antimicrobial peptide
Qing-Quan Ma, Na Dong, An-Shan Shan, Liang Wang, Wan-Ning Hu, Wen-Yu Sun Protein Pept Lett. 2012 Nov;19(11):1144-8. doi: 10.2174/092986612803217132.
A novel α-helical antimicrobial peptide G6 rich in Val/Arg residues has been screened previously. In this study, we further evaluated the biochemical stability, interaction with whole bacteria, and in vivo therapeutic or prophylactic role of the peptide in Salmonella typhimurium-infected mice. The results showed that G6 exhibited strong resistance to pH, heat, and salts. But G6 lost the antimicrobial activity when treated with proteolytic enzymes. G6 had no toxicity on mammalian cell. An intraperitoneal model of sepsis caused by Salmonella typhimurium was established in mice. G6 was administered intraperitoneally 1 h before or after mice were infected with Salmonella typhimurium. For the mice given peptide post-bacterial infection, the mortality of the mice and the peritoneal bacterial counts were significantly lower in the groups that were administered 2.5 mg/kg BW and 5.0 mg/kg BW of G6 (P < 0.05) compared to the PBS-treated group. Similar trend was obtained when G6 was given 1 h prior to Salmonella typhimurium infection. Peptide-membrane experiments showed that G6 was effective in permeabilizing the outer and inner membrane in a dose dependent manner, indicating that the peptide targets the cell membrane. Taken together, the results revealed that the peptide G6 may provide a useful alternative to antibiotic agents to treat or prevent bacterial infections.
2. Structure-function relationship of Val/Arg-rich peptides: effects of net charge and pro on activity
Qingquan Ma, Wenjing Jiao, Yinfeng Lv, Na Dong, Xin Zhu, Anshan Shan Chem Biol Drug Des. 2014 Sep;84(3):348-53. doi: 10.1111/cbdd.12325. Epub 2014 May 14.
Our previous study reported Val/Arg-rich peptides, and the relationship was linear between hydrophobicity and antimicrobial potency within a certain range. Here, we further develop a new series of analogs to investigate the effect of net charge and Pro residue on activity. Replacement of Gly with Ala or Pro led to the decrease in antimicrobial activity. The substitution of Gly with Ala retained its hemolytic activity, while the substitution with Pro significantly decreased the toxicity, suggesting positive effect of Pro on hemolytic activity. The increase in net charge from +4 to +6 significantly improved antimicrobial activity and decreased the hemolysis. However, antibacterial and hemolytic activities were not affected by increasing the net charge from +6 to +8, indicating a moderate net positive charge. The peptides produced larger blue shifts in PE/PG than in PC/cholesterol, suggesting a stronger affinity with negatively charged membrane over zwitterionic membrane. Lowering the net charge or insert of Pro led to the lack of α-helical structure in SDS micelles, which may be correlated with weakened antimicrobial potency. This study indicated that Val/Arg-rich peptides should have moderate net charge and Pro may play a role in reducing the toxicity against red blood cells.
3. Cell selectivity and interaction with model membranes of Val/Arg-rich peptides
Qing-Quan Ma, An-Shan Shan, Na Dong, Yao Gu, Wen-Yu Sun, Wan-Ning Hu, Xing-Jun Feng J Pept Sci. 2011 Jul;17(7):520-6. doi: 10.1002/psc.1360. Epub 2011 Mar 22.
Antimicrobial peptides are major components of the innate self-defence system and a large number of peptides have been designed to study the mechanism of action. In the present study, a small combinatorial library was designed to study whether the biological activity of Val/Arg-rich peptides is associated with targeted cell membranes. The peptides were produced by segregating hydrophilic residues on the polar side and hydrophobic residues on the opposite side. The peptides displayed strong antimicrobial activity against Gram-negative and Gram-positive bacteria, but weak haemolysis even at a concentration of 256 µM. CD spectra showed that the peptides formed α-helical-rich structure in the presence of negatively charged membranes. The tryptophan fluorescence and quenching experiments indicated that the peptides bound preferentially to negatively charged phospholipids over zwitterionic phospholipids, which corresponds well with the biological activity data. In the in vivo experiment, the peptide G6 decreased the bacterial counts in the mouse peritoneum and increased survival after 7 days. Overall, a high binding affinity with negatively charged phospholipids correlated closely with the cell selectivity of the peptides and some peptides in this study may be likely candidates for the development of antibacterial agents.

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