MedKoo Cat#: 596882 | Name: Mvt 101

Description:

WARNING: This product is for research use only, not for human or veterinary use.

Mvt 101 is a peptide inhibitor.

Chemical Structure

Mvt 101
Mvt 101
CAS#125552-93-4

Theoretical Analysis

MedKoo Cat#: 596882

Name: Mvt 101

CAS#: 125552-93-4

Chemical Formula: C35H67N11O8

Exact Mass: 769.5174

Molecular Weight: 769.99

Elemental Analysis: C, 54.60; H, 8.77; N, 20.01; O, 16.62

Price and Availability

This product is currently not in stock but may be available through custom synthesis. To ensure cost efficiency, the minimum order quantity is 1 gram. The estimated lead time is 2 to 4 months, with pricing dependent on the complexity of the synthesis (typically high for intricate chemistries). Quotes for quantities below 1 gram will not be provided. To request a quote, please click the button below. Note: If this product becomes available in stock in the future, pricing will be listed accordingly.
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Synonym
Mvt 101; Mvt-101; Mvt101;
IUPAC/Chemical Name
(S)-N1-((S)-1-amino-5-guanidino-1-oxopentan-2-yl)-2-((2S,5S,8S,11S)-8-((S)-sec-butyl)-2,5-dibutyl-11-((R)-1-hydroxyethyl)-7,10,13-trioxo-3,6,9,12-tetraazatetradecanamido)pentanediamide
InChi Key
MQPXOVRKKPPKFZ-QYKDHROSSA-N
InChi Code
InChI=1S/C35H67N11O8/c1-7-10-13-23(43-33(53)28(20(4)9-3)46-34(54)29(21(5)47)42-22(6)48)19-41-25(14-11-8-2)31(51)45-26(16-17-27(36)49)32(52)44-24(30(37)50)15-12-18-40-35(38)39/h20-21,23-26,28-29,41,47H,7-19H2,1-6H3,(H2,36,49)(H2,37,50)(H,42,48)(H,43,53)(H,44,52)(H,45,51)(H,46,54)(H4,38,39,40)/t20-,21+,23-,24-,25-,26-,28-,29-/m0/s1
SMILES Code
N=C(N)NCCC[C@@H](C(N)=O)NC([C@H](CCC(N)=O)NC([C@H](CCCC)NC[C@@H](NC([C@H]([C@@H](C)CC)NC([C@H]([C@H](O)C)NC(C)=O)=O)=O)CCCC)=O)=O
Appearance
Solid powder
Purity
>98% (or refer to the Certificate of Analysis)
Shipping Condition
Shipped under ambient temperature as non-hazardous chemical. This product is stable enough for a few weeks during ordinary shipping and time spent in Customs.
Storage Condition
Dry, dark and at 0 - 4 C for short term (days to weeks) or -20 C for long term (months to years).
Solubility
Soluble in DMSO
Shelf Life
>2 years if stored properly
Drug Formulation
This drug may be formulated in DMSO
Stock Solution Storage
0 - 4 C for short term (days to weeks), or -20 C for long term (months).
HS Tariff Code
2934.99.9001
More Info

Preparing Stock Solutions

The following data is based on the product molecular weight 769.99 Batch specific molecular weights may vary from batch to batch due to the degree of hydration, which will affect the solvent volumes required to prepare stock solutions.

Recalculate based on batch purity %
Concentration / Solvent Volume / Mass 1 mg 5 mg 10 mg
1 mM 1.15 mL 5.76 mL 11.51 mL
5 mM 0.23 mL 1.15 mL 2.3 mL
10 mM 0.12 mL 0.58 mL 1.15 mL
50 mM 0.02 mL 0.12 mL 0.23 mL
1: Miller M. The early years of retroviral protease crystal structures. Biopolymers. 2010;94(4):521-9. doi: 10.1002/bip.21387. Review. PubMed PMID: 20593466; PubMed Central PMCID: PMC2938048. 2: Johnson EC, Malito E, Shen Y, Pentelute B, Rich D, Florián J, Tang WJ, Kent SB. Insights from atomic-resolution X-ray structures of chemically synthesized HIV-1 protease in complex with inhibitors. J Mol Biol. 2007 Oct 26;373(3):573-86. Epub 2007 Aug 2. PubMed PMID: 17869270; PubMed Central PMCID: PMC2094697. 3: Torbeev VY, Kent SB. Convergent chemical synthesis and crystal structure of a 203 amino acid "covalent dimer" HIV-1 protease enzyme molecule. Angew Chem Int Ed Engl. 2007;46(10):1667-70. PubMed PMID: 17397076. 4: Trylska J, Bała P, Geller M, Grochowski P. Molecular dynamics simulations of the first steps of the reaction catalyzed by HIV-1 protease. Biophys J. 2002 Aug;83(2):794-807. PubMed PMID: 12124265; PubMed Central PMCID: PMC1302187. 5: Siddiqui MI, Kataria S, Ahuja V, Rao GS. A peptide inhibitor of HIV-1 protease using alpha, beta- dehydro residues: a structure based computer model. Indian J Biochem Biophys. 2001 Feb-Apr;38(1-2):90-5. PubMed PMID: 11563339. 6: Trylska J, Antosiewicz J, Geller M, Hodge CN, Klabe RM, Head MS, Gilson MK. Thermodynamic linkage between the binding of protons and inhibitors to HIV-1 protease. Protein Sci. 1999 Jan;8(1):180-95. PubMed PMID: 10210196; PubMed Central PMCID: PMC2144115. 7: Lee CY, Yang PK, Tzou WS, Hwang MJ. Estimates of relative binding free energies for HIV protease inhibitors using different levels of approximations. Protein Eng. 1998 Jun;11(6):429-37. PubMed PMID: 9725621. 8: Geller M, Miller M, Swanson SM, Maizel J. Analysis of the structure of HIV-1 protease complexed with a hexapeptide inhibitor. Part II: Molecular dynamic studies of the active site region. Proteins. 1997 Feb;27(2):195-203. PubMed PMID: 9061783. 9: Miller M, Geller M, Gribskov M, Kent SB. Analysis of the structure of chemically synthesized HIV-1 protease complexed with a hexapeptide inhibitor. Part I: Crystallographic refinement of 2 A data. Proteins. 1997 Feb;27(2):184-94. PubMed PMID: 9061782. 10: King BL, Vajda S, DeLisi C. Empirical free energy as a target function in docking and design: application to HIV-1 protease inhibitors. FEBS Lett. 1996 Apr 8;384(1):87-91. PubMed PMID: 8797810. 11: Verkhivker GM. Empirical free energy calculations of human immunodeficiency virus type 1 protease crystallographic complexes. II. Knowledge-based ligand-protein interaction potentials applied to thermodynamic analysis of hydrophobic mutations. Pac Symp Biocomput. 1996:638-52. PubMed PMID: 9390264. 12: Kroemer RT, Ettmayer P, Hecht P. 3D-quantitative structure-activity relationships of human immunodeficiency virus type-1 proteinase inhibitors: comparative molecular field analysis of 2-heterosubstituted statine derivatives-implications for the design of novel inhibitors. J Med Chem. 1995 Dec 8;38(25):4917-28. PubMed PMID: 8523405. 13: Tossi A, Antcheva N, Romeo D, Miertus S. Development of pseudopeptide inhibitors of HIV-1 aspartic protease: analysis and tuning of the subsite specificity. Pept Res. 1995 Nov-Dec;8(6):328-34. PubMed PMID: 8838416. 14: Verkhivker G, Appelt K, Freer ST, Villafranca JE. Empirical free energy calculations of ligand-protein crystallographic complexes. I. Knowledge-based ligand-protein interaction potentials applied to the prediction of human immunodeficiency virus 1 protease binding affinity. Protein Eng. 1995 Jul;8(7):677-91. PubMed PMID: 8577696. 15: Wagner G. The importance of being floppy. Nat Struct Biol. 1995 Apr;2(4):255-7. PubMed PMID: 7796257. 16: Thompson SK, Murthy KH, Zhao B, Winborne E, Green DW, Fisher SM, DesJarlais RL, Tomaszek TA Jr, Meek TD, Gleason JG, et al. Rational design, synthesis, and crystallographic analysis of a hydroxyethylene-based HIV-1 protease inhibitor containing a heterocyclic P1'--P2' amide bond isostere. J Med Chem. 1994 Sep 16;37(19):3100-7. PubMed PMID: 7932533. 17: Lunney EA, Hagen SE, Domagala JM, Humblet C, Kosinski J, Tait BD, Warmus JS, Wilson M, Ferguson D, Hupe D, et al. A novel nonpeptide HIV-1 protease inhibitor: elucidation of the binding mode and its application in the design of related analogs. J Med Chem. 1994 Aug 19;37(17):2664-77. PubMed PMID: 8064795. 18: Varney MD, Appelt K, Kalish V, Reddy MR, Tatlock J, Palmer CL, Romines WH, Wu BW, Musick L. Crystal-structure-based design and synthesis of novel C-terminal inhibitors of HIV protease. J Med Chem. 1994 Jul 22;37(15):2274-84. PubMed PMID: 8057276. 19: Baca M, Kent SB. Catalytic contribution of flap-substrate hydrogen bonds in "HIV-1 protease" explored by chemical synthesis. Proc Natl Acad Sci U S A. 1993 Dec 15;90(24):11638-42. PubMed PMID: 8265601; PubMed Central PMCID: PMC48039. 20: Caflisch A, Miranker A, Karplus M. Multiple copy simultaneous search and construction of ligands in binding sites: application to inhibitors of HIV-1 aspartic proteinase. J Med Chem. 1993 Jul 23;36(15):2142-67. PubMed PMID: 8340918.