Cas no 129426-47-7 (HIV (gp41) Fragment H-Ala-Val-Gly-Ile-Gly-Ala-OH)
HIV (gp41) Fragment H-Ala-Val-Gly-Ile-Gly-Ala-OH Chemical and Physical Properties
Names and Identifiers
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- L-Alanine,L-alanyl-L-valylglycyl-L-isoleucylglycyl- (9CI)
- H-ALA-VAL-GLY-ILE-GLY-ALA-OH
- HIV (gp41) Fragment
- HIV gp120
- HIV-1 GP41
- Mouse Anti HIV-1 gp41
- Recombinant HIV-1 gp41
- ALA-VAL-GLY-ILE-GLY-ALA
- Polyclonal Rabbit Anti HIV-I gp41
- (2S)-2-[[2-[[(2S,3S)-2-[[2-[[(2S)-2-[[(2S)-2-aminopropanoyl]amino]-3-methylbutanoyl]amino]acetyl]amino]-3-methylpentanoyl]amino]acetyl]amino]propanoic acid
- L-Alanine, L-alanyl-L-valylglycyl-L-isoleucylglycyl-
- AVGIGA
- 129426-47-7
- L-Alanine, L-alanyl-L-valylglycyl-L-isoleucylglycyl- (9CI)
- DTXSID00156152
- N-terminal of gp41 of HIV-1-BH10
- NH2-Ala-Val-Gly-Ile-Gly-Ala-COOH; AVGIGA
- NH2-Ala-Val-Gly-Ile-Gly-Ala-COOH
- HIV (gp41) Fragment H-Ala-Val-Gly-Ile-Gly-Ala-OH
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- Inchi: 1S/C21H38N6O7/c1-7-11(4)17(20(32)24-8-14(28)25-13(6)21(33)34)26-15(29)9-23-19(31)16(10(2)3)27-18(30)12(5)22/h10-13,16-17H,7-9,22H2,1-6H3,(H,23,31)(H,24,32)(H,25,28)(H,26,29)(H,27,30)(H,33,34)/t11-,12-,13-,16-,17-/m0/s1
- InChI Key: KAOCRFBKEXNERP-HLNSEHPISA-N
- SMILES: O=C([C@H]([C@@H](C)CC)NC(CNC([C@H](C(C)C)NC([C@H](C)N)=O)=O)=O)NCC(N[C@H](C(=O)O)C)=O
Computed Properties
- Exact Mass: 486.28044
- Monoisotopic Mass: 486.28019757g/mol
- Isotope Atom Count: 0
- Hydrogen Bond Donor Count: 7
- Hydrogen Bond Acceptor Count: 13
- Heavy Atom Count: 34
- Rotatable Bond Count: 19
- Complexity: 758
- Covalently-Bonded Unit Count: 1
- Defined Atom Stereocenter Count: 5
- Undefined Atom Stereocenter Count : 0
- Defined Bond Stereocenter Count: 0
- Undefined Bond Stereocenter Count: 0
- XLogP3: -4.5
- Topological Polar Surface Area: 209?2
Experimental Properties
- PSA: 208.82
HIV (gp41) Fragment H-Ala-Val-Gly-Ile-Gly-Ala-OH Pricemore >>
| Related Categories | No. | Product Name | Cas No. | Purity | Specification | Price | update time | Inquiry |
|---|---|---|---|---|---|---|---|---|
| TRC | H251885-2.5mg |
HIV (gp41) Fragment H-Ala-Val-Gly-Ile-Gly-Ala-OH |
129426-47-7 | 2.5mg |
$ 400.00 | 2022-06-04 | ||
| TRC | H251885-5mg |
HIV (gp41) Fragment H-Ala-Val-Gly-Ile-Gly-Ala-OH |
129426-47-7 | 5mg |
$ 785.00 | 2022-06-04 | ||
| TRC | H251885-10mg |
HIV (gp41) Fragment H-Ala-Val-Gly-Ile-Gly-Ala-OH |
129426-47-7 | 10mg |
$ 1260.00 | 2022-06-04 | ||
| A2B Chem LLC | AA45352-1mg |
L-Alanine, L-alanyl-L-valylglycyl-L-isoleucylglycyl- (9CI) |
129426-47-7 | > 95% | 1mg |
$318.00 | 2024-04-20 | |
| A2B Chem LLC | AA45352-5mg |
L-Alanine, L-alanyl-L-valylglycyl-L-isoleucylglycyl- (9CI) |
129426-47-7 | > 95% | 5mg |
$495.00 | 2024-04-20 | |
| A2B Chem LLC | AA45352-10mg |
L-Alanine, L-alanyl-L-valylglycyl-L-isoleucylglycyl- (9CI) |
129426-47-7 | > 95% | 10mg |
$642.00 | 2024-04-20 |
HIV (gp41) Fragment H-Ala-Val-Gly-Ile-Gly-Ala-OH Related Literature
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M. Zeiger,N. J?ckel,P. Strubel,L. Borchardt,R. Reinhold,W. Nickel,J. Eckert,V. Presser,S. Kaskel J. Mater. Chem. A, 2015,3, 17983-17990
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Christopher J. Harrison,Kyle J. Berean,Enrico Della Gaspera,Jian Zhen Ou,Richard B. Kaner,Kourosh Kalantar-zadeh,Torben Daeneke Nanoscale, 2016,8, 16276-16283
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Sowmyalakshmi Venkataraman RSC Adv., 2015,5, 73807-73813
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David White,Sean R. Stowell Biomater. Sci., 2017,5, 463-474
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Xiaotong Feng,Lei Bian,Jie Ma,Lei Zhou,Xiayan Wang,Guangsheng Guo,Qiaosheng Pu Chem. Commun., 2019,55, 3963-3966
Additional information on HIV (gp41) Fragment H-Ala-Val-Gly-Ile-Gly-Ala-OH
Recent Advances in HIV (gp41) Fragment H-Ala-Val-Gly-Ile-Gly-Ala-OH and Compound 129426-47-7: Implications for Antiviral Therapy
The HIV (gp41) Fragment H-Ala-Val-Gly-Ile-Gly-Ala-OH and the compound 129426-47-7 have recently garnered significant attention in the field of antiviral research. These molecules are pivotal in the study of HIV entry inhibitors, particularly in targeting the gp41 glycoprotein, which plays a crucial role in viral fusion and entry into host cells. This research brief synthesizes the latest findings on these entities, highlighting their potential applications and mechanistic insights.
The gp41 glycoprotein is a transmembrane subunit of the HIV envelope glycoprotein complex, essential for mediating fusion between the viral and host cell membranes. The hexapeptide fragment H-Ala-Val-Gly-Ile-Gly-Ala-OH corresponds to a conserved region within gp41, known to be involved in the formation of the six-helix bundle during membrane fusion. Recent studies have focused on utilizing this fragment as a template for designing peptide-based inhibitors that can disrupt the fusion process, thereby preventing viral entry.
Compound 129426-47-7, a small molecule with potential antiviral properties, has been investigated for its ability to interfere with gp41-mediated fusion. Preliminary in vitro studies suggest that this compound may bind to specific hydrophobic pockets on gp41, inhibiting conformational changes required for membrane fusion. Structural analyses, including X-ray crystallography and molecular docking simulations, have provided valuable insights into the binding interactions between 129426-47-7 and gp41, offering a foundation for further optimization.
Recent advancements in peptide synthesis and modification techniques have enabled the development of more stable and bioavailable analogs of the gp41 fragment. For instance, cyclization and incorporation of non-natural amino acids have been explored to enhance the proteolytic stability and binding affinity of the peptide. These modifications aim to overcome the limitations associated with natural peptides, such as rapid degradation and poor pharmacokinetics.
In parallel, high-throughput screening and computational modeling have identified several derivatives of 129426-47-7 with improved antiviral activity and reduced cytotoxicity. These efforts are part of a broader strategy to discover next-generation HIV entry inhibitors that can complement existing antiretroviral therapies. Notably, some of these derivatives have shown synergistic effects when combined with other fusion inhibitors, suggesting potential for combination therapy.
The therapeutic potential of targeting gp41 is further underscored by the emergence of drug-resistant HIV strains. Given the high conservation of the gp41 fusion domain, inhibitors targeting this region are less likely to encounter resistance, making them attractive candidates for long-term treatment. Clinical trials involving peptide-based gp41 inhibitors are currently underway, with preliminary results indicating favorable safety profiles and antiviral efficacy.
In conclusion, the ongoing research on HIV (gp41) Fragment H-Ala-Val-Gly-Ile-Gly-Ala-OH and compound 129426-47-7 represents a promising avenue for the development of novel antiviral agents. By elucidating the structural and functional aspects of these molecules, researchers are paving the way for innovative therapeutic strategies to combat HIV infection. Future studies should focus on optimizing the pharmacokinetic properties of these inhibitors and evaluating their efficacy in vivo, with the ultimate goal of translating these findings into clinical applications.
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