Need Assistance?

US & Canada:
+
UK: +

FAQs

Resources

Our Highlights

GMP Grade Efficient workshop for GMP production.
Optimal Prices Buying products on this site guarantees the best price!
Commercial Batches Independent GMP manufacturing suites that handle commercial batches
Prompt Delivery Warehouses in multiple cities to ensure timely delivery
Flexible Quantity Quantities available from milligrams to ton

Application Area

Esculentin-2P

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

Esculentin-2P is produced by Rana pipiens. It has antibacterial activity against Gram-negative bacterium E.coli.

Category

Functional Peptides

Catalog number

BAT-012236

Molecular Formula

C173H290N50O46S2

Molecular Weight

3870.58

Specification
Reference Reading

IUPAC Name

(3S)-3-[[(2S)-6-amino-2-[[2-[[(2S)-2-[[2-[[(2S)-6-amino-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-6-amino-2-[[(2S)-2-[[(2S)-2-[[2-[[(2S)-2-[[(2S)-2-[[(2S,3S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[(2-aminoacetyl)amino]-3-phenylpropanoyl]amino]-3-hydroxypropanoyl]amino]-3-hydroxypropanoyl]amino]-3-methylpentanoyl]amino]-3-phenylpropanoyl]amino]-5-carbamimidamidopentanoyl]amino]acetyl]amino]-3-methylbutanoyl]amino]propanoyl]amino]hexanoyl]amino]-3-phenylpropanoyl]amino]propanoyl]amino]-3-hydroxypropanoyl]amino]hexanoyl]amino]acetyl]amino]-4-methylpentanoyl]amino]acetyl]amino]hexanoyl]amino]-4-[[(2S)-1-[[(2S)-1-[[(2S)-1-[[(2S)-1-[[2-[[(2S)-1-[[(2S)-4-amino-1-[[(2S)-1-[[(2S)-1-[[(2S)-1-[[(2R)-1-[[(2S)-6-amino-1-[[(2S,3S)-1-[[(2S)-1-[[(2S)-6-amino-1-[[(2S)-5-amino-1-[[(1R)-1-carboxy-2-sulfanylethyl]amino]-1,5-dioxopentan-2-yl]amino]-1-oxohexan-2-yl]amino]-3-hydroxy-1-oxopropan-2-yl]amino]-3-methyl-1-oxopentan-2-yl]amino]-1-oxohexan-2-yl]amino]-1-oxo-3-sulfanylpropan-2-yl]amino]-1-oxopropan-2-yl]amino]-3-methyl-1-oxobutan-2-yl]amino]-4-methyl-1-oxopentan-2-yl]amino]-1,4-dioxobutan-2-yl]amino]-3-methyl-1-oxobutan-2-yl]amino]-2-oxoethyl]amino]-4-methyl-1-oxopentan-2-yl]amino]-5-carbamimidamido-1-oxopentan-2-yl]amino]-1-oxopropan-2-yl]amino]-4-methyl-1-oxopentan-2-yl]amino]-4-oxobutanoic acid

Purity

>96% by HPLC

Sequence

GFSSIFRGVAKFASKGLGKDLARLGVNLVACKISKQC

InChI

InChI=1S/C173H290N50O46S2/c1-23-95(17)138(223-164(261)124(85-227)215-163(260)122(83-225)214-156(253)116(197-129(230)77-179)72-101-46-28-25-29-47-101)169(266)211-118(74-103-50-32-27-33-51-103)157(254)201-105(57-44-66-186-172(182)183)145(242)189-80-132(233)219-135(92(11)12)166(263)194-99(21)141(238)199-107(54-36-41-63-176)150(247)209-117(73-102-48-30-26-31-49-102)155(252)193-98(20)142(239)213-121(82-224)161(258)202-104(52-34-39-61-174)144(241)188-79-131(232)198-112(68-88(3)4)146(243)190-78-130(231)196-106(53-35-40-62-175)148(245)210-120(76-134(235)236)159(256)207-114(70-90(7)8)154(251)192-97(19)140(237)200-110(58-45-67-187-173(184)185)151(248)206-113(69-89(5)6)147(244)191-81-133(234)220-136(93(13)14)168(265)212-119(75-128(181)229)158(255)208-115(71-91(9)10)160(257)221-137(94(15)16)167(264)195-100(22)143(240)217-125(86-270)165(262)204-109(56-38-43-65-178)153(250)222-139(96(18)24-2)170(267)216-123(84-226)162(259)203-108(55-37-42-64-177)149(246)205-111(59-60-127(180)228)152(249)218-126(87-271)171(268)269/h25-33,46-51,88-100,104-126,135-139,224-227,270-271H,23-24,34-45,52-87,174-179H2,1-22H3,(H2,180,228)(H2,181,229)(H,188,241)(H,189,242)(H,190,243)(H,191,244)(H,192,251)(H,193,252)(H,194,263)(H,195,264)(H,196,231)(H,197,230)(H,198,232)(H,199,238)(H,200,237)(H,201,254)(H,202,258)(H,203,259)(H,204,262)(H,205,246)(H,206,248)(H,207,256)(H,208,255)(H,209,247)(H,210,245)(H,211,266)(H,212,265)(H,213,239)(H,214,253)(H,215,260)(H,216,267)(H,217,240)(H,218,249)(H,219,233)(H,220,234)(H,221,257)(H,222,250)(H,223,261)(H,235,236)(H,268,269)(H4,182,183,186)(H4,184,185,187)/t95-,96-,97-,98-,99-,100-,104-,105-,106-,107-,108-,109-,110-,111-,112-,113-,114-,115-,116-,117-,118-,119-,120-,121-,122-,123-,124-,125-,126-,135-,136-,137-,138-,139-/m0/s1

InChI Key

XWWLCUJTTQMXGS-JYVXZIQHSA-N

Canonical SMILES

CCC(C)C(C(=O)NC(CO)C(=O)NC(CCCCN)C(=O)NC(CCC(=O)N)C(=O)NC(CS)C(=O)O)NC(=O)C(CCCCN)NC(=O)C(CS)NC(=O)C(C)NC(=O)C(C(C)C)NC(=O)C(CC(C)C)NC(=O)C(CC(=O)N)NC(=O)C(C(C)C)NC(=O)CNC(=O)C(CC(C)C)NC(=O)C(CCCNC(=N)N)NC(=O)C(C)NC(=O)C(CC(C)C)NC(=O)C(CC(=O)O)NC(=O)C(CCCCN)NC(=O)CNC(=O)C(CC(C)C)NC(=O)CNC(=O)C(CCCCN)NC(=O)C(CO)NC(=O)C(C)NC(=O)C(CC1=CC=CC=C1)NC(=O)C(CCCCN)NC(=O)C(C)NC(=O)C(C(C)C)NC(=O)CNC(=O)C(CCCNC(=N)N)NC(=O)C(CC2=CC=CC=C2)NC(=O)C(C(C)CC)NC(=O)C(CO)NC(=O)C(CO)NC(=O)C(CC3=CC=CC=C3)NC(=O)CN

1. The Chinese bamboo leaf odorous frog (Rana (Odorrana) versabilis) and North American Rana frogs share the same families of skin antimicrobial peptides

Tianbao Chen, Mei Zhou, Pingfan Rao, Brian Walker, Chris Shaw Peptides. 2006 Jul;27(7):1738-44. doi: 10.1016/j.peptides.2006.02.009. Epub 2006 Apr 18.

The Chinese bamboo leaf odorous frog (Rana (Odorrana) versabilis) and the North American pickerel frog (Rana palustris) occupy different ecological niches on two different continents with no overlap in geographical distribution. R. palustris skin secretions contain a formidable array of antimicrobial peptides including homologs of brevinin-1, esculentin-1, esculentin-2, ranatuerin-2, a temporin and a family of peptides considered of unique structural attributes when isolated, palustrins 1-3. Here we describe the structures of mature peptides and precursors of eight putative antimicrobial peptides from the skin secretion of the Chinese bamboo leaf odorous frog (Rana (Odorrana) versabilis). Each peptide represents a structural homolog of respective peptide families isolated from R. palustris, including two peptides identical in primary structure to palustrin 1c and palustrin 3b. Additionally, two peptides were found to be structural homologs of ranatuerin 2B and ranatuerin 2P from the closely-related North American species, Rana berlandieri (the Rio Grande leopard frog) and Rana pipiens (the Northern leopard frog), respectively. Both palustrins and ranatuerins have hitherto been considered unique to North American ranid frogs. The use of primary structures of amphibian skin antimicrobial peptides is thus questionable as a taxonomic device or alternatively, the micro-evolution and/or ancestry of ranid frogs is more highly complex than previously thought.

2. Inactivation of viruses infecting ectothermic animals by amphibian and piscine antimicrobial peptides

V G Chinchar, L Bryan, U Silphadaung, E Noga, D Wade, L Rollins-Smith Virology. 2004 Jun 1;323(2):268-75. doi: 10.1016/j.virol.2004.02.029.

The ability of five purified amphibian antimicrobial peptides (dermaseptin-1, temporin A, magainin I, and II, PGLa), crude peptide fractions isolated from the skin of Rana pipiens and R. catesbeiana, and four antimicrobial peptides (AMPs) from hybrid striped bass (piscidin-1N, -1H, -2, and -3) were examined for their ability to reduce the infectivity of channel catfish virus (CCV) and frog virus 3 (FV3). All compounds, with the exception of magainin I, markedly reduced the infectivity of CCV. In contrast to CCV, FV3 was 2- to 4-fold less sensitive to these agents. Similar to an earlier study employing two other amphibian peptides, the agents used here acted rapidly and over a wide, physiologically relevant, temperature range to reduce virus infectivity. These results extend our previous findings and strongly suggest that various amphibian and piscine AMPs may play important roles in protecting fish and amphibians from pathogenic viruses.

3. Antimicrobial peptide defenses of the mountain yellow-legged frog (Rana muscosa)

Louise A Rollins-Smith, Douglas C Woodhams, Laura K Reinert, Vance T Vredenburg, Cheryl J Briggs, Per F Nielsen, J Michael Conlon Dev Comp Immunol. 2006;30(9):831-42. doi: 10.1016/j.dci.2005.10.005. Epub 2005 Nov 9.

The mountain yellow-legged frog (Rana muscosa) inhabits high elevation lakes in California that are largely undisturbed by human activities. In spite of this habitation in remote sites, populations continue to decline. Although predation by non-native fish is one cause for declines, some isolated populations in fishless lakes are suffering new declines. One possible cause of the current wave of declines is the introduction of the pathogenic chytrid fungus (Batrachochytrium dendrobatidis) which invades the adult skin to cause chytridiomycosis. In many amphibian species, the skin is protected by antimicrobial peptides secreted into the mucous. Here we show that R. muscosa produces three previously unknown antimicrobial peptides belonging to the ranatuerin-2 and temporin-1 families of antimicrobial peptides. These three peptides, along with bradykinin, are the most abundant peptides in the skin secretions detected by mass spectrometry. Natural mixtures of peptides and individual purified peptides strongly inhibit chytrid growth. The concentration of total peptides recovered from the skin of frogs following a mild norepinephrine induction is sufficient to inhibit chytrid growth in vitro. A comparison of the species susceptibility to chytridiomycosis and the antichytrid activity of peptides between R. muscosa and R. pipiens suggest that although R. muscosa produces more total skin peptides, it appears to be more vulnerable to B. dendrobatidis in nature. Possible differences in the antimicrobial peptide repertoires and life history traits of the two species that may account for differences in susceptibility are discussed.