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Merck

N5764

Sigma-Aldrich

Nisin from Lactococcus lactis

potency: ≥900 IU/mg

Sinónimos:

Nisin A

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About This Item

Fórmula empírica (notación de Hill):
C143H230N42O37S7
Número de CAS:
Peso molecular:
3354.07
MDL number:
UNSPSC Code:
51102829
PubChem Substance ID:
NACRES:
NA.85

form

powder

Quality Level

potency

≥900 IU/mg

antibiotic activity spectrum

Gram-negative bacteria
Gram-positive bacteria

mode of action

cell membrane | interferes

storage temp.

2-8°C

SMILES string

[H]N[C@@H]([C@@H](C)CC)C(=O)N\C(=C\C)C(=O)N[C@H]1CSC[C@H](NC(=O)[C@H](CC(C)C)NC(=O)C(=C)NC(=O)[C@@H](NC1=O)[C@@H](C)CC)C(=O)N[C@H]2[C@H](C)SC[C@H](NC(=O)CNC(=O)[C@@H]3CCCN3C2=O)C(=O)N[C@H](CCCCN)C(=O)N[C@@H]4[C@@H](C)SC[C@H](NC(=O)CNC(=O)[C@H](CCSC)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](C)NC(=O)CNC4=O)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CCSC)C(=O)N[C@@H](CCCCN)C(=O)N[C@H]5[C@H](C)SC[C@@H]6NC(=O)[C@@H](NC(=O)[C@H](C)NC5=O)[C@H](C)SC[C@H](NC(=O)[C@H](Cc7cnc[nH]7)NC6=O)C(=O)N[C@@H](CO)C(=O)N[C@@H]([C@@H](C)CC)C(=O)N[C@@H](Cc8cnc[nH]8)C(=O)N[C@@H](C(C)C)C(=O)NC(=C)C(=O)N[C@@H](CCCCN)C(O)=O

InChI

1S/C143H230N42O37S7/c1-24-69(11)105(148)135(213)162-82(27-4)118(196)174-94-58-225-59-95(175-123(201)89(48-67(7)8)169-115(193)74(16)158-138(216)107(70(12)25-2)180-132(94)210)133(211)184-112-79(21)229-61-96(160-104(190)56-152-134(212)100-38-34-44-185(100)142(112)220)128(206)164-84(36-29-32-42-145)120(198)182-109-76(18)226-60-97(161-103(189)55-151-117(195)85(39-45-223-22)165-122(200)88(47-66(5)6)168-113(191)72(14)156-102(188)54-153-136(109)214)129(207)171-92(51-101(147)187)125(203)166-86(40-46-224-23)119(197)163-83(35-28-31-41-144)121(199)183-110-77(19)228-63-99-130(208)170-90(49-80-52-149-64-154-80)124(202)176-98(62-227-78(20)111(141(219)177-99)181-116(194)75(17)159-140(110)218)131(209)173-93(57-186)127(205)179-108(71(13)26-3)139(217)172-91(50-81-53-150-65-155-81)126(204)178-106(68(9)10)137(215)157-73(15)114(192)167-87(143(221)222)37-30-33-43-146/h27,52-53,64-72,75-79,83-100,105-112,186H,15-16,24-26,28-51,54-63,144-146,148H2,1-14,17-23H3,(H2,147,187)(H,149,154)(H,150,155)(H,151,195)(H,152,212)(H,153,214)(H,156,188)(H,157,215)(H,158,216)(H,159,218)(H,160,190)(H,161,189)(H,162,213)(H,163,197)(H,164,206)(H,165,200)(H,166,203)(H,167,192)(H,168,191)(H,169,193)(H,170,208)(H,171,207)(H,172,217)(H,173,209)(H,174,196)(H,175,201)(H,176,202)(H,177,219)(H,178,204)(H,179,205)(H,180,210)(H,181,194)(H,182,198)(H,183,199)(H,184,211)(H,221,222)/b82-27+/t69-,70-,71-,72-,75-,76?,77?,78?,79?,83-,84+,85-,86-,87-,88-,89-,90-,91-,92-,93-,94-,95-,96-,97-,98-,99-,100-,105-,106-,107-,108-,109+,110-,111-,112-/m0/s1

InChI key

NVNLLIYOARQCIX-ILAIHEEGSA-N

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General description

Chemical structure: peptide

Application

Nisin is a polycyclic lantibiotic produced by Lactococcus lactis. It is commonly used as a food preservative. It is also used as a selective agent in cell culture for the isolation of gram-negative bacteria, yeast, and molds. Nisin has been used in bioassays to study posttranslational modification.
Used to form targeted pores in cell membranes that are mediated by lipid II. Used to study the assembly and stability of nisin-lipid II pore complexes.

Biochem/physiol Actions

Nisin binds to cell wall precursor lipid components of bacteria and disrupts cell wall production. Nisin alters the cell membrane which results in the leakage of cytoplasmic components and destruction of the proton motive force.
Nisin is an antibiotic with bactericidal action. It binds to the lipid A portion of bacterial lipopolysaccharides and induces pore formation in the membranes of cortex cells from excised sorghum roots.

Mode of Action: Binds to and interferes with the permeability of the cytoplasmic membrane.
Antimicrobial spectrum: Gram-negative and Gram-positive bacteria (requires chelator such as EDTA).

Packaging

Package size based on weight of total solids

Other Notes

Keep container tightly closed in a dry and well-ventilated place. Keep in a dry place.

Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)


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Qi Zhang et al.
Proceedings of the National Academy of Sciences of the United States of America, 109(45), 18361-18366 (2012-10-17)
Lanthionine-containing peptides (lanthipeptides) are a family of ribosomally synthesized and posttranslationally modified peptides containing (methyl)lanthionine residues. Here we present a phylogenomic study of the four currently known classes of lanthipeptide synthetases (LanB and LanC for class I, LanM for class
V Biscola et al.
Meat science, 93(3), 607-613 (2013-01-01)
A Lactococcus lactis subsp. lactis strain (L. lactis 69) capable to produce a heat-stable bacteriocin was isolated from charqui, a Brazilian fermented, salted and sun-dried meat product. The bacteriocin inhibited, in vitro, Listeria monocytogenes, Staphylococcus aureus, several lactic acid bacteria
Evelyn M Molloy et al.
PloS one, 8(3), e58530-e58530 (2013-03-19)
It is becoming increasingly apparent that innovations from the "golden age" of antibiotics are becoming ineffective, resulting in a pressing need for novel therapeutics. The bacteriocin family of antimicrobial peptides has attracted much attention in recent years as a source
Evelyn M Molloy et al.
Biochemical Society transactions, 40(6), 1492-1497 (2012-11-28)
Bacteriocins are bacterially produced peptides or proteins that inhibit the growth of other bacterial strains. They can have a broad (effective against multiple genera) or narrow (effective against specific species) spectrum of activity. The diversity of bacteriocins found in Nature
Michelle M Nerandzic et al.
PloS one, 8(1), e54740-e54740 (2013-01-26)
Germination is the irreversible loss of spore-specific properties prior to outgrowth. Because germinating spores become more susceptible to killing by stressors, induction of germination has been proposed as a spore control strategy. However, this strategy is limited by superdormant spores

Artículos

With bacterial resistance and emerging infectious diseases becoming potential threats to humans, ribosomally synthesized antimicrobial peptides have become a promising focus area in antibiotic research.

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