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AC-AMP1

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AC-AMP1 is an antimicrobial peptide produced by Amaranthus caudatus (Love-lies-bleeding, Inca-wheat). It has antibacterial and antifungal activity.

Category

Functional Peptides

Catalog number

BAT-013203

CAS number

139632-17-0

Specification
Reference Reading

IUPAC Name

(4S)-5-[[(2R)-1-[[(2S)-1-[[(2S)-1-[[2-[[(2S)-1-[[(2R)-1-[(2S)-2-[[(2S)-1-[[2-[[(2S)-1-[[(2R)-1-[[(2R)-1-[[(2S)-1-[[(2S)-5-amino-1-[[(2S)-1-[[2-[[(2S)-1-[2-[[(2R)-2-[[(2S)-2-[[(2S)-6-amino-2-[[(2S)-1-[2-[[(2S)-6-amino-2-[[2-[[(2R)-2-amino-3-sulfanylpropanoyl]amino]acetyl]amino]hexanoyl]amino]acetyl]pyrrolidine-2-carbonyl]amino]hexanoyl]amino]-3-(4-hydroxyphenyl)propanoyl]amino]-3-sulfanylpropanoyl]amino]acetyl]oxy-3-(4-hydroxyphenyl)-1-oxopropan-2-yl]amino]-2-oxoethyl]amino]-1-oxo-3-phenylpropan-2-yl]amino]-1,5-dioxopentan-2-yl]amino]-3-hydroxy-1-oxopropan-2-yl]amino]-1-oxo-3-sulfanylpropan-2-yl]amino]-1-oxo-3-sulfanylpropan-2-yl]amino]-4-methylsulfanyl-1-oxobutan-2-yl]amino]-2-oxoethyl]amino]-3-hydroxy-1-oxopropan-2-yl]carbamoyl]pyrrolidin-1-yl]-1-oxo-3-sulfanylpropan-2-yl]amino]-5-carbamimidamido-1-oxopentan-2-yl]amino]-2-oxoethyl]amino]-5-carbamimidamido-1-oxopentan-2-yl]amino]-3-methyl-1-oxobutan-2-yl]amino]-1-oxo-3-sulfanylpropan-2-yl]amino]-4-[[2-[[(2S)-2-amino-3-methylbutanoyl]amino]acetyl]amino]-5-oxopentanoic acid

Synonyms

Antimicrobial peptide 1, Plant defensin; Val-Gly-Glu-Cys-Val-Arg-Gly-Arg-Cys-Pro-Ser-Gly-Met-Cys-Cys-Ser-Gln-Phe-Gly-Tyr-Cys-Gly-Lys-Gly-Pro-Lys-Tyr-Cys-Gly (Disulfide bridge: Cys4-Cys15, Cys9-Cys21, Cys14-Cys28)

Purity

>98%

Sequence

VGECVRGRCPSGMCCSQFGYCGKGPKYCG (Disulfide bridge: Cys4-Cys15, Cys9-Cys21, Cys14-Cys28)

Storage

Store at -20°C

InChI

InChI=1S/C124H194N38O37S7/c1-63(2)99(129)119(195)140-52-94(171)145-75(34-36-97(174)175)109(185)157-86(61-204)116(192)160-100(64(3)4)120(196)150-72(21-13-40-134-123(130)131)103(179)137-49-92(169)144-73(22-14-41-135-124(132)133)107(183)159-87(62-205)121(197)162-43-16-24-89(162)118(194)154-81(55-163)105(181)139-50-93(170)146-77(37-44-206-5)111(187)156-85(60-203)115(191)158-84(59-202)114(190)153-82(56-164)113(189)148-76(33-35-90(128)167)110(186)151-78(45-65-17-7-6-8-18-65)104(180)138-51-95(172)147-80(47-67-27-31-69(166)32-28-67)122(198)199-98(176)54-142-106(182)83(58-201)155-112(188)79(46-66-25-29-68(165)30-26-66)152-108(184)74(20-10-12-39-126)149-117(193)88-23-15-42-161(88)96(173)53-141-102(178)71(19-9-11-38-125)143-91(168)48-136-101(177)70(127)57-200/h6-8,17-18,25-32,63-64,70-89,99-100,163-166,200-205H,9-16,19-24,33-62,125-127,129H2,1-5H3,(H2,128,167)(H,136,177)(H,137,179)(H,138,180)(H,139,181)(H,140,195)(H,141,178)(H,142,182)(H,143,168)(H,144,169)(H,145,171)(H,146,170)(H,147,172)(H,148,189)(H,149,193)(H,150,196)(H,151,186)(H,152,184)(H,153,190)(H,154,194)(H,155,188)(H,156,187)(H,157,185)(H,158,191)(H,159,183)(H,160,192)(H,174,175)(H4,130,131,134)(H4,132,133,135)/t70-,71-,72-,73-,74-,75-,76-,77-,78-,79-,80-,81-,82-,83-,84-,85-,86-,87-,88-,89-,99-,100-/m0/s1

InChI Key

CRLBLVQWYMUDAS-FBMKYRQTSA-N

Canonical SMILES

CC(C)C(C(=O)NCC(=O)NC(CCC(=O)O)C(=O)NC(CS)C(=O)NC(C(C)C)C(=O)NC(CCCNC(=N)N)C(=O)NCC(=O)NC(CCCNC(=N)N)C(=O)NC(CS)C(=O)N1CCCC1C(=O)NC(CO)C(=O)NCC(=O)NC(CCSC)C(=O)NC(CS)C(=O)NC(CS)C(=O)NC(CO)C(=O)NC(CCC(=O)N)C(=O)NC(CC2=CC=CC=C2)C(=O)NCC(=O)NC(CC3=CC=C(C=C3)O)C(=O)OC(=O)CNC(=O)C(CS)NC(=O)C(CC4=CC=C(C=C4)O)NC(=O)C(CCCCN)NC(=O)C5CCCN5C(=O)CNC(=O)C(CCCCN)NC(=O)CNC(=O)C(CS)N)N

1. Purification, characterization, and sequencing of antimicrobial peptides, Cy-AMP1, Cy-AMP2, and Cy-AMP3, from the Cycad (Cycas revoluta) seeds

Seiya Yokoyama, Kouji Kato, Atsuko Koba, Yuji Minami, Keiichi Watanabe, Fumio Yagi Peptides. 2008 Dec;29(12):2110-7. doi: 10.1016/j.peptides.2008.08.007. Epub 2008 Aug 20.

Novel antimicrobial peptides (AMP), designated Cy-AMP1, Cy-AMP2, and Cy-AMP3, were purified from seeds of the cycad (Cycas revoluta) by a CM cellulofine column, ion-exchange HPLC on SP COSMOGEL, and reverse-phase HPLC. They had molecular masses of 4583.2 Da, 4568.9 Da and 9275.8 Da, respectively, by MALDI-TOF MS analysis. Half of the amino acid residues of Cy-AMP1 and Cy-AMP2 were cysteine, glycine and proline, and their sequences were similar. The sequence of Cy-AMP3 showed high homology to various lipid transfer proteins. For Cy-AMP1 and Cy-AMP2, the concentrations of peptides required for 50% inhibition (IC(50)) of the growth of plant pathogenic fungi, Gram-positive and Gram-negative bacteria were 7.0-8.9 microg/ml. The Cy-AMP3 had weak antimicrobial activity. The structural and antimicrobial characteristics of Cy-AMP1 and Cy-AMP2 indicated that they are a novel type of antimicrobial peptide belonging to a plant defensin family.

2. Purification, characterization, and sequencing of a novel type of antimicrobial peptides, Fa-AMP1 and Fa-AMP2, from seeds of buckwheat (Fagopyrum esculentum Moench.)

Masatoshi Fujimura, Yuji Minami, Keiichi Watanabe, Kenjiro Tadera Biosci Biotechnol Biochem. 2003 Aug;67(8):1636-42. doi: 10.1271/bbb.67.1636.

Novel antimicrobial peptides (AMP), designated Fa-AMP1 and Fa-AMP2, were purified from the seeds of buckwheat (Fagopyrum esculentum Moench.) by gel filtration on Sephadex G75, ion-exchange HPLC on SP COSMOGEL, and reverse-phase HPLC. They were basic peptides having isoelectric points of over 10. Fa-AMP1 and Fa-AMP2 had molecular masses of 3,879 Da and 3,906 Da on MALDI-TOF MS analysis, and their extinction coefficients in 1% aqueous solutions at 280 nm were 42.8 and 38.9, respectively. Half of all amino acid residues of Fa-AMP1 and Fa-AMP2 were cysteine and glycine, and they had continuous sequences of cysteine and glycine. The concentrations of peptides required for 50% inhibition (IC50) of the growth of plant pathogenic fungi, and Gram-positive and -negative bacteria were 11 to 36 microg/ml. The structural and antimicrobial characteristics of Fa-AMPs indicated that they are a novel type of antimicrobial peptides belonging to a plant defensin family.

3. Two hevein homologs isolated from the seed of Pharbitis nil L. exhibit potent antifungal activity

J C Koo, S Y Lee, H J Chun, Y H Cheong, J S Choi, S Kawabata, M Miyagi, S Tsunasawa, K S Ha, D W Bae, C D Han, B L Lee, M J Cho Biochim Biophys Acta. 1998 Jan 15;1382(1):80-90. doi: 10.1016/s0167-4838(97)00148-9.

Two antifungal peptides (Pn-AMP1 and Pn-AMP2) have been purified to homogeneity from seeds of Pharbitis nil. The amino acid sequences of Pn-AMP1 (41 amino acid0 residues) and Pn-AMP2 (40 amino acid residues) were identical except that Pn-AMP1 has an additional serine residue at the carboxyl-terminus. The molecular masses of Pn-AMP1 and Pn-AMP2 were confirmed as 4299.7 and 4213.2 Da, respectively. Both the Pn-AMPs were highly basic (pI 12.02) and had characteristics of cysteine/glycine rich chitin-binding domain. Pn-AMPs exhibited potent antifungal activity against both chitin-containing and non-chitin-containing fungi in the cell wall. Concentrations required for 50% inhibition of fungal growth were ranged from 3 to 26 micrograms/ml for Pn-AMP1 and from 0.6 to 75 micrograms/ml for Pn-AMP2. The Pn-AMPs penetrated very rapidly into fungal hyphae and localized at septum and hyphal tips of fungi, which caused burst of hyphal tips. Burst of hyphae resulted in disruption of the fungal membrane and leakage of the cytoplasmic materials. To our knowledge, Pn-AMPs are the first hevein-like proteins that show similar fungicidal effects as thionins do.