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Uperin 3.6

* Please kindly note that our products are not to be used for therapeutic purposes and cannot be sold to patients.

Uperin 3.6 is a broad-spectrum antibiotic peptide isolated from Uperoleia mjobergii.

Category

Functional Peptides

Catalog number

BAT-010999

Molecular Formula

C86H139N23O20

Molecular Weight

1815.2

Specification
Reference Reading

IUPAC Name

(3S)-3-[[(2S,3S)-2-[[(2S)-2-[(2-aminoacetyl)amino]-3-methylbutanoyl]amino]-3-methylpentanoyl]amino]-4-[[(2S)-1-[[(2S)-1-[[(2S)-6-amino-1-[[(2S)-6-amino-1-[[(2S)-1-[[(2S)-4-amino-1-[[(2S)-1-[[(2S)-1-[[(2S)-6-amino-1-[[(2S)-4-amino-1-[[(2S)-1-[[(2S)-1-amino-1-oxo-3-phenylpropan-2-yl]amino]-4-methyl-1-oxopentan-2-yl]amino]-1,4-dioxobutan-2-yl]amino]-1-oxohexan-2-yl]amino]-4-methyl-1-oxopentan-2-yl]amino]-3-methyl-1-oxobutan-2-yl]amino]-1,4-dioxobutan-2-yl]amino]-3-(1H-indol-3-yl)-1-oxopropan-2-yl]amino]-1-oxohexan-2-yl]amino]-1-oxohexan-2-yl]amino]-1-oxopropan-2-yl]amino]-1-oxopropan-2-yl]amino]-4-oxobutanoic acid

Synonyms

NH2-Gly-Val-Ile-Asp-Ala-Ala-Lys-Lys-Trp-Asn-Val-Leu-Lys-Asn-Leu-Phe-NH2

Purity

>97%

Sequence

GVIDAAKKVVNVLKNLF-NH2

Storage

Store at -20°C

InChI

InChI=1S/C86H139N23O20/c1-13-48(10)71(109-85(128)69(46(6)7)107-67(112)42-90)86(129)106-64(41-68(113)114)78(121)96-49(11)73(116)95-50(12)74(117)97-55(29-19-22-32-87)75(118)98-56(30-20-23-33-88)76(119)102-61(38-52-43-94-54-28-18-17-27-53(52)54)81(124)104-63(40-66(92)111)83(126)108-70(47(8)9)84(127)105-60(36-45(4)5)79(122)99-57(31-21-24-34-89)77(120)103-62(39-65(91)110)82(125)101-59(35-44(2)3)80(123)100-58(72(93)115)37-51-25-15-14-16-26-51/h14-18,25-28,43-50,55-64,69-71,94H,13,19-24,29-42,87-90H2,1-12H3,(H2,91,110)(H2,92,111)(H2,93,115)(H,95,116)(H,96,121)(H,97,117)(H,98,118)(H,99,122)(H,100,123)(H,101,125)(H,102,119)(H,103,120)(H,104,124)(H,105,127)(H,106,129)(H,107,112)(H,108,126)(H,109,128)(H,113,114)/t48-,49-,50-,55-,56-,57-,58-,59-,60-,61-,62-,63-,64-,69-,70-,71-/m0/s1

InChI Key

NMYWNRXIMLMQEQ-LNZTUMAESA-N

Canonical SMILES

CCC(C)C(C(=O)NC(CC(=O)O)C(=O)NC(C)C(=O)NC(C)C(=O)NC(CCCCN)C(=O)NC(CCCCN)C(=O)NC(CC1=CNC2=CC=CC=C21)C(=O)NC(CC(=O)N)C(=O)NC(C(C)C)C(=O)NC(CC(C)C)C(=O)NC(CCCCN)C(=O)NC(CC(=O)N)C(=O)NC(CC(C)C)C(=O)NC(CC3=CC=CC=C3)C(=O)N)NC(=O)C(C(C)C)NC(=O)CN

1. The solution structure of uperin 3.6, an antibiotic peptide from the granular dorsal glands of the Australian toadlet, Uperoleia mjobergii

B C Chia, J A Carver, T D Mulhern, J H Bowie J Pept Res. 1999 Aug;54(2):137-45. doi: 10.1034/j.1399-3011.1999.00095.x.

Uperin 3.6 (GVIDA5AKKVV10NVLKN15LF-NH2) is a wide-spectrum antibiotic peptide isolated from the Australian toadlet, Uperoleia mjobergii. With only 17 amino acid residues, it is smaller than most other wide-spectrum antibiotic peptides isolated from amphibians. In 50% (by vol.) trifluoroethanol, an NMR study and structure calculations indicate that uperin 3.6 adopts a well-defined amphipathic alpha-helix with distinct hydrophilic and hydrophobic faces. Examination of the activities of synthetic modifications of uperin 3.6 reveal that the three lysine residues are essential for antibiotic activity.

2. In vitro activity and killing effect of uperin 3.6 against gram-positive cocci isolated from immunocompromised patients

Andrea Giacometti, et al. Antimicrob Agents Chemother. 2005 Sep;49(9):3933-6. doi: 10.1128/AAC.49.9.3933-3936.2005.

The in vitro activity of uperin 3.6, alone or combined with six antibiotics, against gram-positive cocci, including Rhodococcus equi, methicillin-resistant staphylococci, and vancomycin-resistant enterococci, was investigated. All isolates were inhibited at concentrations of 1 to 16 mg/liter. Synergy was demonstrated when uperin 3.6 was combined with clarithromycin and doxycycline.

3. Activity of Novel Synthetic Peptides against Candida albicans

Kah Yean Lum, Sun Tee Tay, Cheng Foh Le, Vannajan Sanghiran Lee, Nadia Hanim Sabri, Rukumani Devi Velayuthan, Hamimah Hassan, Shamala Devi Sekaran Sci Rep. 2015 May 12;5:9657. doi: 10.1038/srep09657.

Candida spp. are the most common causes of fungal infections worldwide. Among the Candida species, Candida albicans remains the predominant species that causes invasive candidiasis in most countries. In this study, we used two peptides, KABT-AMP and uperin 3.6 as templates to develop novel antifungal peptides. Their anticandidal activity was assessed using a combination of MIC, time-killing assay and biofilm reduction assay. Hybrid peptides, KU2 and KU3 containing a mixed backbone of KABT-AMP and Uperin 3.6 demonstrated the most potent anticandidal activity with MIC values ranging from 8-16 mg/L. The number of Trp residues and the amphipathic structure of peptides probably enhanced the anticandidal activity of peptides. Increasing the cationicity of the uperin 3.6 analogues resulted in reduced MIC from the range of 64-128 mg/L to 16-64 mg/L and this was also correlated with the antibiofilm activity and killing kinetics of the peptides. Peptides showed synergistic effects when used in combination with conventional antifungals. Peptides demonstrated low haemolytic activity but significant toxicity on two normal human epithelial cell lines. This study provides us with a better understanding on the structure-activity relationship and the balance between cationicity and hydrophobicity of the peptides although the therapeutic application of the peptides is limited.