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Ceratotoxin B

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Ceratotoxin B is an antimicrobial peptide produced by the sexually mature female of Ceratitis capitata.

Category

Functional Peptides

Catalog number

BAT-009353

CAS number

150671-05-9

Molecular Formula

C135H235N35O32

Molecular Weight

2860.53

Specification
Reference Reading

IUPAC Name

(2S)-1-[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-6-amino-2-[[(2S)-2-[[(2S,3S)-2-[[(2S)-1-[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-6-amino-2-[[2-[[(2S,3S)-2-[[(2S)-6-amino-2-[[(2S)-6-amino-2-[[(2S)-2-[[(2S)-2-[[(2S)-1-[(2S)-2-[[(2S)-2-[[(2S)-6-amino-2-[[(2S)-6-amino-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[2-[[(2S,3S)-2-[[(2S)-2-amino-3-hydroxypropanoyl]amino]-3-methylpentanoyl]amino]acetyl]amino]-3-hydroxypropanoyl]amino]propanoyl]amino]-3-phenylpropanoyl]amino]hexanoyl]amino]hexanoyl]amino]propanoyl]amino]-4-methylpentanoyl]pyrrolidine-2-carbonyl]amino]-3-methylbutanoyl]amino]propanoyl]amino]hexanoyl]amino]hexanoyl]amino]-3-methylpentanoyl]amino]acetyl]amino]hexanoyl]amino]propanoyl]amino]propanoyl]amino]-4-methylpentanoyl]pyrrolidine-2-carbonyl]amino]-3-methylpentanoyl]amino]propanoyl]amino]hexanoyl]amino]propanoyl]amino]propanoyl]amino]-4-methylpentanoyl]pyrrolidine-2-carboxylic acid

Synonyms

Ser-Ile-Gly-Ser-Ala-Phe-Lys-Lys-Ala-Leu-Pro-Val-Ala-Lys-Lys-Ile-Gly-Lys-Ala-Ala-Leu-Pro-Ile-Ala-Lys-Ala-Ala-Leu-Pro; L-Proline, L-seryl-L-isoleucylglycyl-L-seryl-L-alanyl-L-phenylalanyl-L-lysyl-L-lysyl-L-alanyl-L-leucyl-L-prolyl-L-valyl-L-alanyl-L-lysyl-L-lysyl-L-isoleucylglycyl-L-lysyl-L-alanyl-L-alanyl-L-leucyl-L-prolyl-L-isoleucyl-L-alanyl-L-lysyl-L-alanyl-L-alanyl-L-leucyl-; Ceratotoxin B protein, Ceratitis capitata

Appearance

White or Off-white Lyophilized Powder

Purity

≥95% by HPLC

Sequence

SIGSAFKKALPVAKKIGKAALPIAKAALP

Storage

Store at -20°C

Solubility

Soluble in DMSO, Water

InChI

InChI=1S/C135H235N35O32/c1-23-76(12)106(165-117(183)88(142)70-171)128(194)144-69-104(174)154-99(71-172)125(191)150-83(19)113(179)160-95(67-87-44-27-26-28-45-87)124(190)159-93(50-33-39-59-140)122(188)157-91(48-31-37-57-138)120(186)149-84(20)116(182)162-97(65-73(6)7)132(198)168-61-41-52-100(168)126(192)164-105(75(10)11)130(196)151-85(21)111(177)156-92(49-32-38-58-139)121(187)158-94(51-34-40-60-141)123(189)166-107(77(13)24-2)129(195)143-68-103(173)153-89(46-29-35-55-136)118(184)147-79(15)109(175)145-81(17)114(180)161-96(64-72(4)5)133(199)169-62-42-53-101(169)127(193)167-108(78(14)25-3)131(197)152-86(22)112(178)155-90(47-30-36-56-137)119(185)148-80(16)110(176)146-82(18)115(181)163-98(66-74(8)9)134(200)170-63-43-54-102(170)135(201)202/h26-28,44-45,72-86,88-102,105-108,171-172H,23-25,29-43,46-71,136-142H2,1-22H3,(H,143,195)(H,144,194)(H,145,175)(H,146,176)(H,147,184)(H,148,185)(H,149,186)(H,150,191)(H,151,196)(H,152,197)(H,153,173)(H,154,174)(H,155,178)(H,156,177)(H,157,188)(H,158,187)(H,159,190)(H,160,179)(H,161,180)(H,162,182)(H,163,181)(H,164,192)(H,165,183)(H,166,189)(H,167,193)(H,201,202)/t76-,77-,78-,79-,80-,81-,82-,83-,84-,85-,86-,88-,89-,90-,91-,92-,93-,94-,95-,96-,97-,98-,99-,100-,101-,102-,105-,106-,107-,108-/m0/s1

InChI Key

LZXMDTIXCKHFGQ-NBKZZIEESA-N

Canonical SMILES

CCC(C)C(C(=O)NC(C)C(=O)NC(CCCCN)C(=O)NC(C)C(=O)NC(C)C(=O)NC(CC(C)C)C(=O)N1CCCC1C(=O)O)NC(=O)C2CCCN2C(=O)C(CC(C)C)NC(=O)C(C)NC(=O)C(C)NC(=O)C(CCCCN)NC(=O)CNC(=O)C(C(C)CC)NC(=O)C(CCCCN)NC(=O)C(CCCCN)NC(=O)C(C)NC(=O)C(C(C)C)NC(=O)C3CCCN3C(=O)C(CC(C)C)NC(=O)C(C)NC(=O)C(CCCCN)NC(=O)C(CCCCN)NC(=O)C(CC4=CC=CC=C4)NC(=O)C(C)NC(=O)C(CO)NC(=O)CNC(=O)C(C(C)CC)NC(=O)C(CO)N

1. Purification and primary structure of ceratotoxin A and B, two antibacterial peptides from the female reproductive accessory glands of the medfly Ceratitis capitata (Insecta:Diptera)

D Marchini, P C Giordano, R Amons, L F Bernini, R Dallai Insect Biochem Mol Biol. 1993 Jul;23(5):591-8. doi: 10.1016/0965-1748(93)90032-n.

In the present article we report the purification and the amino acid sequence of two antibacterial peptides present in the secretion of the female reproductive accessory glands of the dipteran insect Ceratitis capitata. Both peptides consist of 29 amino acid residues, are heat stable, strongly basic and differ from each other for the substitution of two amino acids. Their primary sequence and predicted secondary structure are related to other families of peptides known to have lytic and/or antibacterial activity. We propose the name ceratotoxins (from Ceratitis) for these antibacterial peptides.

2. The genes encoding the antibacterial sex-specific peptides ceratotoxins are clustered in the genome of the medfly Ceratitis capitata

M Rosetto, T De Filippis, A G Manetti, D Marchini, C T Baldari, R Dallai Insect Biochem Mol Biol. 1997 Dec;27(12):1039-46. doi: 10.1016/s0965-1748(97)00090-8.

Ceratotoxins are antibacterial peptides produced in the female reproductive accessory glands of the medfly Ceratitis capitata. Their expression is not affected by bacterial infection, but is enhanced after mating and is modulated by juvenile hormone. Three different peptides, named ceratotoxins A, B and C, have been previously purified from the female accessory gland secretion and their amino acid and cDNA sequences have been determined. We report here the complete nucleotide sequences of four genes encoding closely related ceratotoxin peptides. One of them encodes a novel peptide, which we named ceratotoxin D. Restriction and nucleotide sequence analysis indicate that these ceratotoxin genes are organized in a large cluster spanning more than 26 kilobases of DNA. All ceratotoxin genes are coordinately expressed. Ceratotoxin transcripts appear in 2-3 day old adult females, and they reach a maximum in 6-7 day old females. The presence of highly conserved motifs in the upstream regions of all the sequenced ceratotoxin genes suggests the presence of common regulatory elements for all ceratotoxins.

3. CD and NMR structural characterization of ceratotoxins, natural peptides with antimicrobial activity

L Ragona, H Molinari, L Zetta, R Longhi, D Marchini, R Dallai, L F Bernini, L Lozzi, M Scarselli, N Niccolai Biopolymers. 1996 Nov;39(5):653-64. doi: 10.1002/(SICI)1097-0282(199611)39:5%3C653::AID-BIP4%3E3.0.CO;2-V.

Antibacterial properties of the secretion from the female reproductive accessory glands of medfly Ceratitis capitata are mostly ascribed to the presence of two peptides, ceratotoxin A and B, which exhibit a strong activity against gram-positive and gram-negative bacterial strains, and show sequence and function homology with cecropins, melittin, and magainins. CD experiments performed in different solvents indicate the presence of a significant content of helical structures in organic solvent. Two-dimensional nmr results for ceratotoxin A in methanol show a helical behavior for the 8-25 region of the peptide. A ramachandran classification of each residue for the structures obtained from distance geometry calculations lead to the definition of four structural families in which the central segment 10-19 is always helical and differences refer to residues 8-9 and 19-23. A sequence analysis of the two ceratotoxins and a systematic search on the protein data bank revealed the occurrence of a KX-hydrophobic-hydrophobic-P motif that seems to be important for helix stabilization.